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2fkg

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[[Image:2fkg.gif|left|200px]]
[[Image:2fkg.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2fkg", creates the "Structure Box" on the page.
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{{STRUCTURE_2fkg| PDB=2fkg | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkg OCA], [http://www.ebi.ac.uk/pdbsum/2fkg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fkg RCSB]</span>
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'''The Crystal Structure of Engineered OspA'''
'''The Crystal Structure of Engineered OspA'''
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==About this Structure==
==About this Structure==
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2FKG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKG OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKG OCA].
==Reference==
==Reference==
Atomic structures of peptide self-assembly mimics., Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, Koide A, Koide S, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17753-8. Epub 2006 Nov 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17093048 17093048]
Atomic structures of peptide self-assembly mimics., Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, Koide A, Koide S, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17753-8. Epub 2006 Nov 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17093048 17093048]
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[[Category: Borrelia burgdorferi]]
 
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[[Category: Protein complex]]
 
[[Category: Gawlak, G.]]
[[Category: Gawlak, G.]]
[[Category: Koide, S.]]
[[Category: Koide, S.]]
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[[Category: Terechko, V.]]
[[Category: Terechko, V.]]
[[Category: Yan, S.]]
[[Category: Yan, S.]]
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[[Category: beta sheet]]
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[[Category: Beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:00:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:04:02 2008''
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Revision as of 01:00, 4 May 2008

Image:2fkg.gif

Template:STRUCTURE 2fkg

The Crystal Structure of Engineered OspA


Overview

Although the beta-rich self-assemblies are a major structural class for polypeptides and the focus of intense research, little is known about their atomic structures and dynamics due to their insoluble and noncrystalline nature. We developed a protein engineering strategy that captures a self-assembly segment in a water-soluble molecule. A predefined number of self-assembling peptide units are linked, and the beta-sheet ends are capped to prevent aggregation, which yields a mono-dispersed soluble protein. We tested this strategy by using Borrelia outer surface protein (OspA) whose single-layer beta-sheet located between two globular domains consists of two beta-hairpin units and thus can be considered as a prototype of self-assembly. We constructed self-assembly mimics of different sizes and determined their atomic structures using x-ray crystallography and NMR spectroscopy. Highly regular beta-sheet geometries were maintained in these structures, and peptide units had a nearly identical conformation, supporting the concept that a peptide in the regular beta-geometry is primed for self-assembly. However, we found small but significant differences in the relative orientation between adjacent peptide units in terms of beta-sheet twist and bend, suggesting their inherent flexibility. Modeling shows how this conformational diversity, when propagated over a large number of peptide units, can lead to a substantial degree of nanoscale polymorphism of self-assemblies.

About this Structure

Full crystallographic information is available from OCA.

Reference

Atomic structures of peptide self-assembly mimics., Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, Koide A, Koide S, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17753-8. Epub 2006 Nov 8. PMID:17093048 Page seeded by OCA on Sun May 4 04:00:06 2008

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