Proteopedia - User contributions [en]

G13secL03Tpc3

2012-08-16T15:05:48Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that reside in the gut of hard- bodied deer tick of the family ''Ixodidae''. They are transmitted in humans by the bite of this tick. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref> The structure and stability of Osp B is affected by this antibody causing the bacteria to lyse.

==Structure==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Final_ospb/2'/>
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Final_bsheet/2'/>

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

===Interactions===
The structure of Osp B shows that there are three exposed loops that are affected by the antibody, H6831. The majority of interaction occurs between the antibody’s heavy chain and <scene name='G13secL03Tpc3/Loop_2_final/1'>Loop 2</scene> on the lipoprotein, residues 250-254. The loop forms electrostatic interaction and hydrogen bond interactions with the antibody's heavy chain. Lysine 253, which resides on Loop 2, plays an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. The Lysine interacts with the antibody by forming hydrogen bonds with the glutamine and histidine on the heavy chain of H6831. <scene name='G13secL03Tpc3/Loop_1/1'>Loop 1</scene>, residues 231-233, also interacts with the Fab heavy chain by forming two hydrogen bonds. <scene name='G13secL03Tpc3/Loop_3_final/2'>Loop 3</scene>, residues 272-276, interacts with the Fab light chain of the antibody with two hydrogen bonds. <ref name=Article2> PMID:15864264 </ref> Loop 3 contains Threonine 276, an amino acid that, along with Lysine 253, contributes most to the contact and binding of H6831 to OspB.

==Structural changes==
A more significant <scene name='G13secL03Tpc3/Final_bsheet/3'>structural change</scene> that occurs during the bactericidal Fab complex is the removal of OspB's first four beta sheets. Surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the outer surface protein and make the bacteria more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly. The proteolytic activity of the antibody on the bacteria is presumably similar to a [http://en.wikipedia.org/wiki/Complement_membrane_attack_complex membrane attack complex] (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
Under pressure in the presence of antibodies, OspB is capable of existing in various forms. Mutations occur in the residue of Lysine 253, the epitope of H6831, and may prevent ''Borrelia'' from being recognized and lysed by bactericidal Fabs such as H6381. <ref name=Article4> PMID: 15128807 </ref> The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines created to specifically fight OspB have not yet been successful, due to the increased variability of the epitope. Vaccine are not yet able to counteract the varied strains of ''Borrelia burgdorferi.'' However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research, as it is still currently misunderstood.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T17:32:22Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/1' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Ospb/2' />

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref>

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T17:25:35Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/1' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='Generalstructure1' />

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref>

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T17:23:50Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Ospb/2' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/1'
/>

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref>

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T17:17:45Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Ospb_c_terminus/2' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/1'
/>

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref>

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T17:15:52Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/1/1' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/1'
/>

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref>

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T14:41:29Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

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

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Ospb_c_terminus/2' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13secL03Tpc3

2012-08-14T14:38:35Z

Sonia Araujo:

G13secL03Tpc3

2012-08-14T14:38:05Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

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

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene= G13secL03Tpc3/Ospb_c_terminus/2>

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13secL03Tpc3

2012-08-14T14:37:34Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

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

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene= G13secL03Tpc3/Ospb_c_terminus/2 />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13secL03Tpc3

2012-08-14T14:36:50Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

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

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='G13secL03Tpc3/Ospb_c_terminus/2 />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13secL03Tpc3

2012-08-14T14:35:58Z

Sonia Araujo:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

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

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='G13secL03Tpc3/Ospb_c_terminus/2' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.