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| - | [[Image:2i5z.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2i5z| PDB=2i5z | SCENE= }} | | {{STRUCTURE_2i5z| PDB=2i5z | SCENE= }} |
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| - | '''The crystal structure of OspA mutant'''
| + | ===The crystal structure of OspA mutant=== |
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| - | ==Overview==
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| - | Formation of a flat beta-sheet is a fundamental event in beta-sheet-mediated protein self-assembly. To investigate the contributions of various factors to the stability of flat beta-sheets, we performed extensive alanine-scanning mutagenesis experiments on the single-layer beta-sheet segment of Borrelia outer surface protein A (OspA). This beta-sheet segment consists of beta-strands with highly regular geometries that can serve as a building block for self-assembly. Our Ala-scanning approach is distinct from the conventional host-guest method, in that it introduces only conservative, truncation mutations that should minimize structural perturbation. Our results showed very weak correlation with experimental beta-sheet propensity scales, statistical beta-sheet propensity scales, or cross-strand pairwise correlations. In contrast, our data showed strong positive correlation with the change in buried non-polar surface area. Polar interactions including prominent Glu-Lys cross-strand pairs contribute marginally to the beta-sheet stability. These results were corroborated by results from additional non-Ala mutations. Taken together, these results demonstrate the dominant contribution of non-polar surface burial to flat beta-sheet stability even at solvent-exposed positions. The OspA single-layer beta-sheet achieves efficient hydrophobic surface burial without forming a hydrophobic core by a strategic placement of a variety of side-chains. These findings further suggest the importance of hydrophobic interactions within a beta-sheet layer in peptide self-assembly.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17335845}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17335845 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17335845}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Terechko, V.]] | | [[Category: Terechko, V.]] |
| | [[Category: Beta-sheet]] | | [[Category: Beta-sheet]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:07:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:45:39 2008'' |
Revision as of 12:45, 29 July 2008
Template:STRUCTURE 2i5z
The crystal structure of OspA mutant
Template:ABSTRACT PUBMED 17335845
About this Structure
2I5Z is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.
Reference
Hydrophobic surface burial is the major stability determinant of a flat, single-layer beta-sheet., Yan S, Gawlak G, Makabe K, Tereshko V, Koide A, Koide S, J Mol Biol. 2007 Apr 20;368(1):230-43. Epub 2007 Feb 7. PMID:17335845
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