2af5
From Proteopedia
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[[Image:2af5.gif|left|200px]] | [[Image:2af5.gif|left|200px]] | ||
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'''2.5A X-ray Structure of Engineered OspA protein''' | '''2.5A X-ray Structure of Engineered OspA protein''' | ||
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[[Category: Mcelheny, D.]] | [[Category: Mcelheny, D.]] | ||
[[Category: Tereshko, V.]] | [[Category: Tereshko, V.]] | ||
| - | [[Category: | + | [[Category: Beta-hairpin]] |
| - | [[Category: | + | [[Category: Repeat protein]] |
| - | [[Category: | + | [[Category: Single-layer beta-sheet]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:58:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:58, 3 May 2008
2.5A X-ray Structure of Engineered OspA protein
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
2AF5 is a Single protein structure of sequence from Borrelia burgdorferi. 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 Sat May 3 18:58:17 2008
