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| - | [[Image:2ol8.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2ol8| PDB=2ol8 | SCENE= }} | | {{STRUCTURE_2ol8| PDB=2ol8 | SCENE= }} |
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| - | '''The crystal structure of OspA mutant'''
| + | ===The crystal structure of OspA mutant=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17985889}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17985889 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17985889}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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 11:08:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:41:16 2008'' |
Revision as of 12:41, 29 July 2008
Template:STRUCTURE 2ol8
The crystal structure of OspA mutant
Template:ABSTRACT PUBMED 17985889
About this Structure
2OL8 is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.
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:17985889
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