1mtp: Difference between revisions
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<StructureSection load='1mtp' size='340' side='right' caption='[[1mtp]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1mtp' size='340' side='right' caption='[[1mtp]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mtp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1mtp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MTP FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mtp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mtp RCSB], [http://www.ebi.ac.uk/pdbsum/1mtp PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mtp OCA], [http://pdbe.org/1mtp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mtp RCSB], [http://www.ebi.ac.uk/pdbsum/1mtp PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1mtp" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Thermonospora fusca henssen 1957]] | ||
[[Category: Bottomley, S P]] | [[Category: Bottomley, S P]] | ||
[[Category: Cabrita, L D]] | [[Category: Cabrita, L D]] | ||
Revision as of 13:27, 11 September 2015
The X-ray crystal structure of a serpin from a thermophilic prokaryoteThe X-ray crystal structure of a serpin from a thermophilic prokaryote
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSerpins utilize conformational change to inhibit target proteinases; the price paid for this conformational flexibility is that many undergo temperature-induced polymerization. Despite this thermolability, serpins are present in the genomes of thermophilic prokaryotes, and here we characterize the first such serpin, thermopin. Thermopin is a proteinase inhibitor and, in comparison with human alpha(1)-antitrypsin, possesses enhanced stability at 60 degrees C. The 1.5 A crystal structure reveals novel structural features in regions implicated in serpin folding and stability. Thermopin possesses a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These data provide evidence as to how this unusual serpin has adapted to fold and function in a heated environment. The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment.,Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC Structure. 2003 Apr;11(4):387-97. PMID:12679017[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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