2ol6: Difference between revisions

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|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=[[2ol7|2OL7]], [[2ol8|2OL8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ol6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ol6 OCA], [http://www.ebi.ac.uk/pdbsum/2ol6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ol6 RCSB]</span>
}}
}}


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[[Category: membrane protein]]
[[Category: membrane protein]]


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Revision as of 04:19, 31 March 2008

File:2ol6.jpg


PDB ID 2ol6

Drag the structure with the mouse to rotate
, resolution 1.60Å
Gene: ospA (Borrelia burgdorferi)
Related: 2OL7, 2OL8


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

2OL6 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

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