2ol8: Difference between revisions
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[[Image:2ol8.jpg|left|200px]] | [[Image:2ol8.jpg|left|200px]] | ||
'''The crystal structure of OspA mutant''' | {{Structure | ||
|PDB= 2ol8 |SIZE=350|CAPTION= <scene name='initialview01'>2ol8</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | |||
}} | |||
'''The crystal structure of OspA mutant''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OL8 is a [ | 2OL8 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=2OL8 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17985889 17985889] | ||
[[Category: Borrelia burgdorferi]] | [[Category: Borrelia burgdorferi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:01:10 2008'' | ||
Revision as of 19:01, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Gene: | ospA (Borrelia burgdorferi) | ||||||
| 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
2OL8 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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