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2ol7

From Proteopedia

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{{Seed}}
 
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[[Image:2ol7.png|left|200px]]
 
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==The crystal structure of OspA mutant==
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The line below this paragraph, containing "STRUCTURE_2ol7", creates the "Structure Box" on the page.
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<StructureSection load='2ol7' size='340' side='right'caption='[[2ol7]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ol7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OL7 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ol7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ol7 OCA], [https://pdbe.org/2ol7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ol7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ol7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ol7 ProSAT]</span></td></tr>
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{{STRUCTURE_2ol7| PDB=2ol7 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ol/2ol7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ol7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===The crystal structure of OspA mutant===
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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<ref>PMID:17985889</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ol7" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17985889}}, adds the Publication Abstract to the page
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*[[Outer surface protein|Outer surface protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17985889 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17985889}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Borreliella burgdorferi]]
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2OL7 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=2OL7 OCA].
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[[Category: Large Structures]]
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[[Category: Koide S]]
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==Reference==
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[[Category: Makabe K]]
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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]
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[[Category: Terechko V]]
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[[Category: Borrelia burgdorferi]]
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[[Category: Single protein]]
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[[Category: Koide, S.]]
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[[Category: Makabe, K.]]
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[[Category: Terechko, V.]]
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[[Category: Beta-sheet]]
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[[Category: Membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:57:45 2008''
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Current revision

The crystal structure of OspA mutant

PDB ID 2ol7

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