1f1m

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(New page: 200px<br /><applet load="1f1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f1m, resolution 1.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1f1m.gif|left|200px]]<br /><applet load="1f1m" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f1m.gif|left|200px]]<br /><applet load="1f1m" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f1m, resolution 1.80&Aring;" />
caption="1f1m, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN C (OSPC)'''<br />
'''CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN C (OSPC)'''<br />
==Overview==
==Overview==
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Outer surface protein C (OspC) is a major antigen on the surface of the, Lyme disease spirochete, Borrelia burgdorferi, when it is being, transmitted to humans. Crystal structures of OspC have been determined for, strains HB19 and B31 to 1.8 and 2.5 A resolution, respectively. The, three-dimensional structure is predominantly helical. This is in contrast, to the structure of OspA, a major surface protein mainly present when, spirochetes are residing in the midgut of unfed ticks, which is mostly, beta-sheet. The surface of OspC that would project away from the, spirochete's membrane has a region of strong negative electrostatic, potential which may be involved in binding to positively charged host, ligands. This feature is present only on OspCs from strains known to cause, invasive human disease.
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Outer surface protein C (OspC) is a major antigen on the surface of the Lyme disease spirochete, Borrelia burgdorferi, when it is being transmitted to humans. Crystal structures of OspC have been determined for strains HB19 and B31 to 1.8 and 2.5 A resolution, respectively. The three-dimensional structure is predominantly helical. This is in contrast to the structure of OspA, a major surface protein mainly present when spirochetes are residing in the midgut of unfed ticks, which is mostly beta-sheet. The surface of OspC that would project away from the spirochete's membrane has a region of strong negative electrostatic potential which may be involved in binding to positively charged host ligands. This feature is present only on OspCs from strains known to cause invasive human disease.
==About this Structure==
==About this Structure==
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1F1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F1M OCA].
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1F1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1M OCA].
==Reference==
==Reference==
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[[Category: Borrelia burgdorferi]]
[[Category: Borrelia burgdorferi]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dunn, J.J.]]
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[[Category: Dunn, J J.]]
[[Category: Eswaramoorthy, S.]]
[[Category: Eswaramoorthy, S.]]
[[Category: Kumaran, D.]]
[[Category: Kumaran, D.]]
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[[Category: ospc]]
[[Category: ospc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:08:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:49 2008''

Revision as of 10:33, 21 February 2008


1f1m, resolution 1.80Å

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CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN C (OSPC)

Overview

Outer surface protein C (OspC) is a major antigen on the surface of the Lyme disease spirochete, Borrelia burgdorferi, when it is being transmitted to humans. Crystal structures of OspC have been determined for strains HB19 and B31 to 1.8 and 2.5 A resolution, respectively. The three-dimensional structure is predominantly helical. This is in contrast to the structure of OspA, a major surface protein mainly present when spirochetes are residing in the midgut of unfed ticks, which is mostly beta-sheet. The surface of OspC that would project away from the spirochete's membrane has a region of strong negative electrostatic potential which may be involved in binding to positively charged host ligands. This feature is present only on OspCs from strains known to cause invasive human disease.

About this Structure

1F1M is a Single protein structure of sequence from Borrelia burgdorferi with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi., Kumaran D, Eswaramoorthy S, Luft BJ, Koide S, Dunn JJ, Lawson CL, Swaminathan S, EMBO J. 2001 Mar 1;20(5):971-8. PMID:11230121

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