2i5v
From Proteopedia
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|PDB= 2i5v |SIZE=350|CAPTION= <scene name='initialview01'>2i5v</scene>, resolution 1.10Å | |PDB= 2i5v |SIZE=350|CAPTION= <scene name='initialview01'>2i5v</scene>, resolution 1.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene> | + | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | |GENE= ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i5v OCA], [http://www.ebi.ac.uk/pdbsum/2i5v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i5v RCSB]</span> | ||
}} | }} | ||
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[[Category: Makabe, K.]] | [[Category: Makabe, K.]] | ||
[[Category: Terechko, V.]] | [[Category: Terechko, V.]] | ||
| - | [[Category: PG4]] | ||
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
[[Category: de novo protein]] | [[Category: de novo protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:40:08 2008'' |
Revision as of 00:40, 31 March 2008
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| , resolution 1.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ospA (Borrelia burgdorferi) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of OspA mutant
Overview
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.
About this Structure
2I5V 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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