Proteopedia - User contributions [en]

Polygalacturonase

2017-07-13T18:35:55Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Tertiary structure of ''endo''-polygalacturonase II' scene='Tertiary structure of ''endo''-polygalacturonase II' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectates – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectates in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).

--MDY -- this is a bit confusing. PG's are found in bacteria, fungi, plants, and animals. Plant PG's are involved in fruit ripening. Bacteria and fungal PG are involved in plant pathogenesis, often acting as plant virulence factors and involved in some of the initial pathogenic effects through their action of degrading the plant cell wall. -- MDY

== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

MDY -- we need to distinguish between pectate and pectin. Pectate is a galacturonate polymer, pectin has a polygalacturonate backbone, but some of the monomers are methylesterified on the sixth carbon. PG acts on pectate, not pectin -- MDY

== Disease ==

== Relevance ==

== Structural highlights ==

The tertiary fold of PGs varies in its composition of coils, approximating at 10 coils in a right-handed parallel beta helix domain along with loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands. Nomenclature on how the sheets and turns are labeled are described in Yoder et al <ref>PMID:8081738</ref>.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils. [[Image:PBH2.jpg|200px|left|thumb| Nomenclature for structural elements of the parallel beta helix<ref>PMID:8081738</ref>. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[PBH2]]]] With the parallel beta helix fold, the three major beta sheets are call PB1, PB2, and PB3. The turns between strands are Turn 1 (T1) between PB1 and PB2, T2 is the turn between PB2 and PB3, and T3 is the turn between PB3 and PB1 of the next coil. For your reference, this is illustrated in the figure below.
--MDY

== References ==
<references/>
<ref>Pickersgill, R., Smith D., Worboys K., and Jenkins, J. "Crystal Structure of Polygalacturonase from Erwinia carotovora ssp. carotovora." The Jorunal of Biological Chemistry June (1998). [http://dx.doi.org/10.1074/jbc.273.38.24660 DOI: 10.1074/jbc.273.38.24660]</ref>

File:PBH2.jpg

2017-07-13T14:12:24Z

Marilyn Yoder: schematic of parallel beta helix fold

== Summary ==
schematic of parallel beta helix fold
== Licensing ==
{{PD-self}}

Polygalacturonase

2017-07-13T00:43:26Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).

--MDY -- this is a bit confusing. PG's are found in bacteria, fungi, plants, and animals. Plant PG's are involved in fruit ripening. Bacteria and fungal PG are involved in plant pathogenesis, often acting as plant virulence factors and involved in some of the initial pathogenic effects through their action of degrading the plant cell wall. -- MDY

== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

MDY -- we need to distinguish between pectate and pectin. Pectate is a galacturonate polymer, pectin has a polygalacturonate backbone, but some of the monomers are methylesterified on the sixth carbon. PG acts on pectate, not pectin -- MDY

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils. [[Image:Phb.jpg|200px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[Pbh]]]] With the parallel beta helix fold, the three major beta sheets are call PB1, PB2, and PB3. The turns between strands are Turn 1 (T1) between PB1 and PB2, T2 is the turn between PB2 and PB3, and T3 is the turn between PB3 and PB1 of the next coil. For your reference, this is illustrated in the figure below.
--MDY

== References ==
<references/>

Polygalacturonase

2017-07-13T00:42:14Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).

--MDY -- this is a bit confusing. PG's are found in bacteria, fungi, plants, and animals. Plant PG's are involved in fruit ripening. Bacteria and fungal PG are involved in plant pathogenesis, often acting as plant virulence factors and involved in some of the initial pathogenic effects through their action of degrading the plant cell wall. -- MDY

== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

MDY -- we need to distinguish between pectate and pectin. Pectate is a galacturonate polymer, pectin has a polygalacturonate backbone, but some of the monomers are methylesterified on the sixth carbon. PG acts on pectate, not pectin -- MDY

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils. [[Image:Phb.jpg|300px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[Pbh]]]] With the parallel beta helix fold, the three major beta sheets are call PB1, PB2, and PB3. The turns between strands are Turn 1 (T1) between PB1 and PB2, T2 is the turn between PB2 and PB3, and T3 is the turn between PB3 and PB1 of the next coil. For your reference, this is illustrated in the figure below.
--MDY

== References ==
<references/>

Polygalacturonase

2017-07-13T00:36:03Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).
== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

MDY -- we need to distinguish between pectate and pectin. Pectate is a galacturonate polymer, pectin has a polygalacturonate backbone, but some of the monomers are methylesterified on the sixth carbon. PG acts on pectate, not pectin -- MDY

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils. [[Image:Phb.jpg|300px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[Pbh]]]] With the parallel beta helix fold, the three major beta sheets are call PB1, PB2, and PB3. The turns between strands are Turn 1 (T1) between PB1 and PB2, T2 is the turn between PB2 and PB3, and T3 is the turn between PB3 and PB1 of the next coil. For your reference, this is illustrated in the figure below.
--MDY

== References ==
<references/>

Polygalacturonase

2017-07-13T00:13:02Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).
== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils. [[Image:Phb.jpg|300px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[Pbh]]]] With the parallel beta helix fold, the three major beta sheets are call PB1, PB2, and PB3. The turns between strands are Turn 1 (T1) between PB1 and PB2, T2 is the turn between PB2 and PB3, and T3 is the turn between PB3 and PB1 of the next coil. For your reference, this is illustrated in the figure below.
--MDY

== References ==
<references/>

Polygalacturonase

2017-07-12T23:49:30Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).
== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils. With the parallel beta helix fold, the three major beta sheets are call PB1, PB2, and PB3. The turns between strands are Turn 1 (T1) between PB1 and PB2, T2 is the turn between PB2 and PB3, and T3 is the turn between PB3 and PB1 of the next coil. For your reference, this is illustrated in the figure below.
[[Image:Phb.jpg|300px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[Pbh]]]]

== References ==
<references/>

Polygalacturonase

2017-07-12T23:48:05Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).
== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils. With the parallel beta helix fold, the three major beta sheets are call PB1, PB2, and PB3. The turns between strands are Turn 1 (T1) between PB1 and PB2, T2 is the turn between PB2 and PB3, and T3 is the turn between PB3 and PB1 of the next coil.
[[Image:Phb.jpg|300px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[Pbh]]]]

== References ==
<references/>

Polygalacturonase

2017-07-12T20:53:39Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).
== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils.
[[Image:Phb.jpg|300px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2., [[Pbh]]]]

== References ==
<references/>

File:Phb.jpg

2017-07-12T20:51:28Z

Marilyn Yoder:

Polygalacturonase

2017-07-12T20:50:23Z

Marilyn Yoder:

<Structure load='1czf' size='350' frame='true' align='right' caption='Secondary structure of ''endo''-polygalacturonase II' scene='Insert optional scene name here' />Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by ''exo-'' and ''endo-'' PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function). Microbial PGs have been identified to be a part of defense mechanisms because of their role in pathogen attack (crystal structure).
== Function ==

Polygalacturonases hydrolyze α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues in polygalacturonic acids. Structural variation has been identified among differing PGs depending on organismal origins and catalytic functions. For example, endo-polygalacturonases produced from Erwinia carotovora demonstrate functional similarity to pectate lyases in that they cleave polygalacturonic acids in a calcium-depended manner via β-elimination (crystal structure).

== Disease ==

== Relevance ==

== Structural highlights ==

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity (crystal structure).

MDY- a right-handed parallel beta helix is a tertiary fold. The secondary structure is the beta and the alpha structure. If you describe how the secondary structure folds in space, that becomes tertiary structure. The secondary structural elements of the core fold of the proteins are only beta structure, the beta strands form parallel beta sheets. There are three main parallel beta sheets, PG's often have a smaller parallel beta sheet of only three-four beta strands.

Not all PGs have ten coils in the parallel beta helix. They usually have approximately 10 coils.
[[Image:phb.jpg|300px|left|thumb| Nomenclature for structural elements of the parallel beta helix. PB1 is Parallel Beta Sheet 1, T1 is Turn 1, between PB1 and PB2. ]]

== References ==
<references/>

File:PBH.jpg

2017-07-12T20:47:11Z

Marilyn Yoder:

Polygalacturonase

2017-07-12T20:44:05Z

Marilyn Yoder:

Polygalacturonase

2017-07-12T20:11:00Z

Marilyn Yoder:

Polygalacturonase

2017-06-28T20:02:27Z

Marilyn Yoder:

==Your Heading Here (maybe something like 'Structure')== 0
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 354'''. 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 ==
this is where you describe the function
== Disease ==
Hi Krishna !!

== 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/>

Polygalacturonase

2017-06-13T21:33:46Z

Marilyn Yoder:

==Your Heading Here (maybe something like 'Structure')== 0
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved 354'''. 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 ==
this is where you describe the 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/>

Sandbox Yoder

2017-03-30T18:36:00Z

Marilyn Yoder:

==Pectate Lyases==
<StructureSection load='2ewe' size='340' side='right' caption='Pectate Lyases' scene=''>
This is a default text for your page '''Sandbox Yoder'''. 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 ==
Pecate lyases cleave the alpha 1,4 glycosidic bond in polygalacturonate, pectate, polysaccharides.
== 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.

== Sructures from the PDB ==
As of Apr, 2017
1air
2ewe
1plc

== Other related links ==
Cazy.org

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

Sandbox Yoder

2017-03-30T16:20:28Z

Marilyn Yoder:

Sandbox Yoder

2017-03-30T16:19:22Z

Marilyn Yoder:

==Pectate Lyases== 0
<StructureSection load='2ewe' size='340' side='right' caption='Pectate Lyases' scene=''>
This is a default text for your page '''Sandbox Yoder'''. 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/>

Sandbox Yoder

2017-03-30T16:18:41Z

Marilyn Yoder: New page: ==Your Heading Here (maybe something like 'Structure')== 0 <StructureSection load='2ewe' size='340' side='right' caption='Pectate Lyases' scene=''> This is a default text for your page '''...

==Your Heading Here (maybe something like 'Structure')== 0
<StructureSection load='2ewe' size='340' side='right' caption='Pectate Lyases' scene=''>
This is a default text for your page '''Sandbox Yoder'''. 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/>

Sandbox 352

2017-03-30T16:13:02Z

Marilyn Yoder:

==Pectate Lyases==
<StructureSection load='1stp' size='340' side='right' caption='Pectate Lyase attempt 2' scene=''>
This is a default text for your page '''Sandbox 352'''. 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/>

Sandbox 352

2017-03-30T16:12:18Z

Marilyn Yoder: New page: ==Pectate Lyases== 0 <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for your page '''Sandbox 352'''. Click abov...

==Pectate Lyases== 0
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox 352'''. 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/>