Proteopedia - User contributions [en]

User:Luis Netto/Sandbox 1

2019-06-10T17:01:10Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption overall Ohr structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others

== Disease ==

related with relevance

== Relevance ==

Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].

== Structural highlights ==

Ohr is a homo-dimer, with a symmetrical,oval shape. The two monomers are tightly wrapped around each other in a head-to-tail orientation to generate a compact quaternary structure (Figure 1).

[[Image:Homodimer_Ohr.png|thumb|Figure1 Ohr homodimer]]

In Figure 1, one monomer is depicted in light blue the other in green. Reactive Cys also called peroxidatic Cys (Cp) is depicted in orange. Catalytic Arg (red) and Glu (pink) compose the catalytic triad with Cp. The catalytic Glu orientates the catalytic Arg towards Cp, increasing its nucleophilicity.

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

The structures of Ohr in the reduced and oxidized form were also obtained. For Ohr from Xylella fastidiosa the structures of both reduced and oxidized are available.

<scene name='78/785321/Oxidized_ohr/1'>Text To Be Displayed</scene>

== References ==
<references/>

User:Luis Netto/Sandbox 1

2019-06-10T14:35:47Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption overall Ohr structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others

== Disease ==

related with relevance

== Relevance ==

Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].

== Structural highlights ==

Ohr is a homo-dimer, with a symmetrical,oval shape. The two monomers are tightly wrapped around each other in a head-to-tail orientation to generate a compact quaternary structure (Figure 1).

[[Image:Homodimer_Ohr.png|thumb|Figure1 Ohr homodimer]]

In Figure 1, one monomer is depicted in light blue the other in green. Reactive Cys also called peroxidatic Cys (Cp) is depicted in orange. Catalytic Arg (red) and Glu (pink) compose the catalytic triad with Cp. The catalytic Glu orientates the catalytic Arg towards Cp, increasing its nucleophilicity.

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

The structures of Ohr in the oxidized form were also obtained. For Ohr from Xylella fastidiosa the structures of both reduced and oxidized are available.

== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-31T21:45:04Z

Luis Netto:

User:Luis Netto/Sandbox 1

2018-05-31T21:39:48Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption overall Ohr structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others

==Your Heading Here (maybe something like 'Structure')==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

related with relevance

== Relevance ==

Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].

== Structural highlights ==

Ohr is a homo-dimer, with a symmetrical,oval shape. The two monomers are tightly wrapped around each other in a head-to-tail orientation to generate a compact quaternary structure.

[[Image:Homodimer_Ohr.png|thumb|Figure1 Ohr homodimer]]

One monomer is depicted in light blue the other in green. Reactive Cys also called peroxidatic Cys (CP) is depicted in orange. Catalytic Arg (red) and Glu (pink) compose the catalytic triad with CP

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-31T21:20:42Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption overall Ohr structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others

==Your Heading Here (maybe something like 'Structure')==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

related with relevance

== Relevance ==

Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].

== Structural highlights ==

Ohr is a homo-dimer, with a symmetrical,oval shape. The two monomers are tightly wrapped around each other in a head-to-tail orientation to generate a compact quaternary structure.

[[Image:Homodimer_Ohr.png|thumb]]

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-31T21:07:26Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption overall Ohr structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others

==Your Heading Here (maybe something like 'Structure')==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

related with relevance

== Relevance ==

Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].

== Structural highlights ==

Ohr is a homo-dimer, with a symmetrical,oval shape. The two monomers are tightly wrapped around each other in a head-to-tail orientation to generate a compact quaternary structure.[[Image:Homodimer_Ohr.png]]

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-31T21:06:14Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption overall Ohr structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others

==Your Heading Here (maybe something like 'Structure')==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

related with relevance

== Relevance ==

Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].

== Structural highlights ==

Ohr is a homo-dimer, with a symmetrical,oval shape. The two monomers are tightly wrapped around each other in a head-to-tail orientation to generate a compact quaternary structure.[[Image:Homodimer_Ohr.png]]

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

Ohr is a tight homo-dimer a

== References ==
<references/>

File:Homodimer Ohr.png

2018-05-31T20:31:42Z

Luis Netto: picture describing the homodimer

picture describing the homodimer

User:Luis Netto/Sandbox 1

2018-05-31T15:56:00Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.

Ohr is a tight homo-dimer a [[Image:Ohr_black_white.png | thumb]]

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others

==Your Heading Here (maybe something like 'Structure')==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

related with relevance

== Relevance ==

Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].

== Structural highlights ==

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-31T15:52:41Z

Luis Netto:

User:Luis Netto/Sandbox 1

2018-05-31T15:36:17Z

Luis Netto:

User:Luis Netto/Sandbox 1

2018-05-31T14:33:20Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide.

Ohr is a tight homo-dimer a [[Image:Ohr_black_white.png | thumb]]

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1ZB8' size='350' side='right' caption='Escherichia coli reca protein-bound DNA (PDB entry [[3rec]])' scene=''>

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

== Relevance ==

== Structural highlights ==

Arg19 and Glu 50 of one chain (lets say chain A) compose the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain B).

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-31T14:19:02Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide.

Ohr is a tight homo-dimer a [[Image:Ohr_black_white.png | thumb]]

glu arg in the active site represent the <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene>

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1ZB8' size='350' side='right' caption='Escherichia coli reca protein-bound DNA (PDB entry [[3rec]])' scene=''>

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-29T21:12:52Z

Luis Netto:

==Ohr ==
<StructureSection load='1ZB8' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide.

Ohr is a tight homo-dimer a [[Image:Ohr_black_white.png | thumb]]

glu arg in the active site

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1ZB8' size='350' side='right' caption='Escherichia coli reca protein-bound DNA (PDB entry [[3rec]])' scene=''>

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

It is involved in the response of

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-05-29T20:49:58Z

Luis Netto:

Collagen Structure & Function

2018-05-19T13:15:29Z

Luis Netto:

<StructureSection load='1cag' size='450' side='right' scene='Sandbox_168/Default/3' caption=''>
==Introduction==
[[Collagen]] is a member of a family of naturally occurring proteins. It is one of the most plentiful proteins present in mammals and it is responsible for performing a variety of important biological functions. It is most well-known for the structural role it plays in the body. It is present in large quantities in connective tissue and provides tendons and ligaments with tensile strength and skin with elasticity. It often works in conjuction with other important proteins such as keratin and elastin.

==Biosynthesis==
Collagen synthesis begins specialized cells called fibroblasts <ref name="biosyn">PMID:PMC1367617</ref>. It is here that amino acids undergo activation; Proline is hydroxylated to Hydroxyproline and Lysine to Hydroxylysine. Peptide subunits of ~250 residues are assembled on the ribosome and are linked by carbohydrate residues to form α-chains <ref name="biosyn" />. Three α-chains then associate with each other and then further associate extracelluarly forming a molecule with a molecular weight of 360,000 <ref name="biosyn" />. Bonds are further strengthened thus forming the insoluble collagen fibril <ref name="biosyn" /> <ref name="collalike" />. During the process of collagen synthesis, free-hydroxyproline and hydroxylysine peptides appear as by-products, some of which are metabolized and may appear in urine <ref name="biosyn" />.

==Molecular Structure==
The shape and structural properties of a native collagen molecule are established by its triple-helical α-domain(s). In classical collagen molecules a single triple-helical domain is observed to compose close to 95% of the molecule.<ref name="residues">PMID:19853297</ref>. However there are also other types of collagens that exist which have been shown to comprise of multiple triple-helical α-domains which only account for a fraction of the molecule's overall mass.

The triple-helical domain structure of collagens consists of three distinct α-chains and earns collagen the name "tropocollagen" <ref name="collalike">PMID:7695699</ref>. Each of these chains contain a characteristic L-handed amino acid sequence of polyproline, often termed as polyproline type II helix <ref>PMID: 19344236</ref>. The proper folding of each of these chains requires a glycine residue to be present in every third position in the polypeptide chain. For example, each α-chain is composed of multiple triplet sequences of of Gly-Y-Z in which Y and Z can be any amino acid. Y is commonly found as proline and Z is usually present as hydroxyproline (Figure 1.). The presence of hydroxyproline in the Y position is also thought to contribute to the stability of the helical form <ref name="collalike" />.

These three α-chains are then twisted around one another in a rope-like manner to produce the overall tightly packed triple-helical form of the molecule. The interaction of α-chains is stabilized via interchain hydrogen bonding making the molecule fairly resistant to attack by other molcules. Each α-chain is surrounded by a hydration sphere which allows a hydrogen bonding network to be present between the water molecules and the peptide acceptor groups.<ref name="collalike" />. This hydrogen bonding occurs when the amino group (NH) of a glycine residue forms a peptide bond with the carbonyl (C=0) of an adjacent residue. The overall molecule is approxiametly 300nm long and 1.5-2nm in diameter.<ref name="collalike" />.
The image on the right-hand side has each side chain colored a different color to shown how each individual <scene name='Sandbox_168/Helices/1'>helices</scene> interact with the others to form the overall molecule. The <scene name='Sandbox_168/Myscene/1'>active sites</scene>
have also been illustrated to point out their positions in the triple-helix.

[[Image:collagen_(alpha_chain).jpg |400px| thumb |'''Figure 1.''' Amino Acid residues in collagen. Gly, Pro and Hydroxyproline residues present in a collagen molecule <ref name="residues"/>.]]
{{Clear}}
==Function==
There are close to 30 different types of collagen that have been identified so far.<ref name="types">PMID:17581806</ref>.
The most abundant type of collagen present in the human body is that of Type I <ref name="types" /> with significant amounts of Type II,III and IV also accounted for.

*Collagen I- found in bones,tendons,organs
*Collagen II- found mainly in cartilage
*Collagen III- found mainly in reticular fibres
*Collagen IV- found in the basement membrane of cell membranes
*Collagen V- found in hair,nails

==Collagen-Related Disorders==
There are many types of disorders associated with collagen.These disorders typically occur as a result of improper folding of these molecules and occasionally due to a particular amino acid substitution <ref name="collalike" />. These include:
*Elhers-Danlos Syndrome (IV)

*Alport Syndrome (IV)

*Osteogenesis imperfecta (I)
-more commonly known as Brittle Bone disease

*Chondrodysplasias (II)

*Atopic Dermatitis (III)
</StructureSection>
==References==
<references/>

User:Luis Netto/Sandbox 1

2018-05-03T21:16:19Z

Luis Netto:

File:Ohr fully oxidized.pdb

2018-05-03T21:04:09Z

Luis Netto: TESTE

TESTE

File:1HD2.pdb

2018-05-03T20:57:52Z

Luis Netto: uploaded a new version of "Image:1HD2.pdb": test

User:Luis Netto/Sandbox 1

2018-05-03T20:35:23Z

Luis Netto:

==Ohr ==
<StructureSection load='1tp' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]]is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide than for organic hydroperoxides.

It is involved in the response of

Ohr is a dimer glu arg in the active site [[Image:Ohr_black_white.png | thumb]]

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-04-28T22:32:34Z

Luis Netto:

==Ohr ==
<StructureSection load='1tp' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein) is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide than for organic hydroperoxides.

It is involved in the response of

Ohr is a dimer glu arg in the active site [[Image:Ohr_black_white.png | thumb]]

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-04-28T22:25:46Z

Luis Netto:

==Ohr ==
<StructureSection load='1tp' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[http://www.proteopedia.org/wiki/index.php/1zb9] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

that display higher preference for hydrogen peroxide than for organic hydroperoxides.

It is involved in the response of

Ohr is a dimer glu arg in the active site [[Image:Ohr_black_white.png | thumb]]

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

File:Ohr black white.png

2018-04-28T21:52:52Z

Luis Netto: dimer ohr

dimer ohr

User:Luis Netto/Sandbox 1

2018-04-18T21:19:48Z

Luis Netto:

==Ohr ==
<StructureSection load='1tp' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[http://proteopedia.org/wiki/index.php/1zb9] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>[[Image:]]

that display higher preference for hydrogen peroxide than for organic hydroperoxides.

It is involved in the response of

Ohr is a dimer glu arg in the active site [[Image:Image:Ohr global view whit.png]]

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Hugo Heringer de Almeida/5YGH

2018-04-12T19:58:03Z

Luis Netto:

<Structure load='5YGH' size='350' frame='true' align='right' caption='Insert caption here' scene='78/781908/Surface_5ygh/1' /> Crystal structure of ZIKV C protein at a resolution of 1.9Å.The structure 5YGH has in total <scene name='78/781908/5ygh_2chain/1'>2 chain</scene>. These are represented by 1 sequence-unique entity. The ZIKV C protein structure contains <scene name='78/781908/All_loop/1'> four α helices</scene> with a long <scene name='78/781908/Pre_a1_loop/1'>pre-α1 loop</scene> and forms dimers. The unique long pre-α1 loop in ZIKV C contributes to the tighter association of dimeric assembly and renders a divergent hydrophobic feature at the lipid bilayer interface in comparison with the known C structures of West Nile and dengue viruses. We reported the interaction between the ZIKV C protein and lipid droplets through confocal microscopy analysis. Substitutions of key amino acids in the pre-α1 loop of ZIKV C disrupted the interaction with lipid droplets, indicating that the loop is critical for membrane association. We also recognized that ZIKV C protein possesses broad binding capability to different nucleotide types, including single-stranded and double-stranded RNAs or DNAs. Furthermore, the highly positively charged interface, mainly formed by α4 helix, is proposed to be responsible for nucleotide binding.

test test

== Function ==
Structure of the capsid protein from Zika Virus.
== Disease ==
Zika
== Relevance ==
These findings will greatly enhance our understanding of ZIKV C protein, providing information for anti-ZIKV drug design targeting the C protein.
== References ==
Shang Z., Song H., Shi Y., Qi J., Gao GF. Crystal Structure of the Capsid Protein from Zika Virus. DOI: 10.1016/j.jmb.2018.02.006

==OBS.:==
This article is a small test for a biochemistry class in University of São Paulo

User:Luis Netto/Sandbox 1

2018-04-11T21:31:04Z

Luis Netto:

==Ohr ==
<StructureSection load='1tp' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[http://proteopedia.org/wiki/index.php/1zb9] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>[[Image:]]

Ohr is a dimer glu arg in the active site [[Image:Image:Ohr global view whit.png]]

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

File:Ohr global view whit.png

2018-04-11T21:26:15Z

Luis Netto: global view Ohr - 1ZB9

global view Ohr - 1ZB9

User:Luis Netto/Sandbox 1

2018-04-11T20:53:30Z

Luis Netto:

==Ohr ==
<StructureSection load='1tp' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein)[http://proteopedia.org/wiki/index.php/1zb9] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>[[Image:]]

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-04-11T20:40:41Z

Luis Netto:

==Ohr ==
<StructureSection load='1tp' size='340' side='right' caption='Caption for this structure' scene=''>

Ohr (Organic Hydroperoxide Resistance Protein) is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>

This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-04-11T20:27:48Z

Luis Netto:

==Ohr (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto/Sandbox 1

2018-04-11T19:32:32Z

Luis Netto: New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Luis Netto

2018-04-11T19:27:34Z

Luis Netto:

* Full Real Name: Luis Eduardo Soares Netto

* Position: Professor

* Institution (NO ABBREVIATIONS): Instituto Biociencias - Uinversidade de Sao Paulo

* City, State/Province, Country: Sao Paulo SP BRAZIL

* Field of Expertise or Study: redox biology - antioxidant proteins

*[[User:Luis Netto/Sandbox 1]]

File:1HD2.pdb

2018-03-22T20:41:51Z

Luis Netto: