2oy1: Difference between revisions

Revision as of 11:54, 4 May 2008

The crystal structure of OspA mutant

OverviewOverview

We investigated how the register between adjacent beta-strands is specified using a series of mutants of the single-layer beta-sheet (SLB) in Borrelia OspA. The single-layer architecture of this system eliminates structural restraints imposed by a hydrophobic core, enabling us to address this question. A critical turn (turn 9/10) in the SLB was replaced with a segment with an intentional structural mismatch. Its crystal structure revealed a one-residue insertion into the central beta-strand (strand 9) of the SLB. This insertion triggered a surprisingly large-scale structural rearrangement: (i) the central strand (strand 9) was shifted by one residue, causing the strand to flip with respect to the adjacent beta-strands and thus completely disrupting the native side-chain contacts; (ii) the three-residue turn located on the opposite end of the beta-strand (turn 8/9) was pushed into its preceding beta-strand (strand 8); (iii) the register between strands 8 and 9 was shifted by three residues. Replacing the original sequence for turn 8/9 with a stronger turn motif restored the original strand register but still with a flipped beta-strand 9. The stability differences of these distinct structures were surprisingly small, consistent with an energy landscape where multiple low-energy states with different beta-sheet configurations exist. The observed conformations can be rationalized in terms of maximizing the number of backbone H-bonds. These results suggest that adjacent beta-strands "stick" through the use of factors that are not highly sequence specific and that beta-strands could slide back and forth relatively easily in the absence of external elements such as turns and tertiary packing.

About this StructureAbout this Structure

2OY1 is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.

ReferenceReference

Beta-strand flipping and slipping triggered by turn replacement reveal the opportunistic nature of beta-strand pairing., Makabe K, Yan S, Tereshko V, Gawlak G, Koide S, J Am Chem Soc. 2007 Nov 28;129(47):14661-9. Epub 2007 Nov 7. PMID:17985889 Page seeded by OCA on Sun May 4 11:54:34 2008

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OCA

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 [[Image:2oy1.jpg|left|200px]]
- {{Structure
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-|GENE= ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi])
+-->
-|DOMAIN=
+{{STRUCTURE_2oy1|  PDB=2oy1  |  SCENE=  }}
-|RELATEDENTRY=[[2ol6|2OL6]], [[2ol7|2OL7]], [[2ol8|2OL8]], [[2oy5|2OY5]], [[2oy7|2OY7]], [[2oy8|2OY8]], [[2oyb|2OYB]]
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oy1 OCA], [http://www.ebi.ac.uk/pdbsum/2oy1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oy1 RCSB]</span>
-}}
 '''The crystal structure of OspA mutant'''
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 [[Category: Makabe, K.]]
 [[Category: Terechko, V.]]
-[[Category: beta-sheet]]
+[[Category: Beta-sheet]]
-[[Category: membrane protein]]
+[[Category: Membrane protein]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:54:34 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:24:54 2008''