We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2i5v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 12: Line 12:
-
==Overview==
+
{{ABSTRACT_18367205}}
-
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==
==About this Structure==
2I5V is a [[Single protein]] structure of sequence 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=2I5V OCA].
2I5V is a [[Single protein]] structure of sequence 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=2I5V 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:[http://www.ncbi.nlm.nih.gov/pubmed/17335845 17335845]
 
[[Category: Borrelia burgdorferi]]
[[Category: Borrelia burgdorferi]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 28: Line 24:
[[Category: De novo protein]]
[[Category: De novo protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 15:05:55 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 18:38:38 2008''

Revision as of 15:38, 25 June 2008

Image:2i5v.png

Template:STRUCTURE 2i5v

Crystal structure of OspA mutant


Template:ABSTRACT 18367205

About this Structure

2I5V is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.

Page seeded by OCA on Wed Jun 25 18:38:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i5v"
Personal tools