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2fkg
From Proteopedia
(New page: 200px<br /><applet load="2fkg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fkg, resolution 2.40Å" /> '''The Crystal Structur...) |
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| - | [[Image:2fkg.gif|left|200px]]<br /><applet load="2fkg" size=" | + | [[Image:2fkg.gif|left|200px]]<br /><applet load="2fkg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fkg, resolution 2.40Å" /> | caption="2fkg, resolution 2.40Å" /> | ||
'''The Crystal Structure of Engineered OspA'''<br /> | '''The Crystal Structure of Engineered OspA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FKG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http:// | + | 2FKG is a [http://en.wikipedia.org/wiki/Protein_complex 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]. |
==Reference== | ==Reference== | ||
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[[Category: beta sheet]] | [[Category: beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:42:13 2008'' |
Revision as of 11:42, 23 January 2008
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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
2FKG is a Protein complex structure of sequences 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
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