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1mtp
From Proteopedia
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==The X-ray crystal structure of a serpin from a thermophilic prokaryote== | ==The X-ray crystal structure of a serpin from a thermophilic prokaryote== | ||
| - | <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 [ | + | <table><tr><td colspan='2'>[[1mtp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1MTP FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <table> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mtp OCA], [https://pdbe.org/1mtp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mtp RCSB], [https://www.ebi.ac.uk/pdbsum/1mtp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mtp ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q47NK3_THEFY Q47NK3_THEFY] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mt/1mtp_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mt/1mtp_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=1mtp ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Serpins 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. | ||
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| - | 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<ref>PMID:12679017</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[Serpin|Serpin]] | + | *[[Serpin 3D structures|Serpin 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thermobifida fusca]] | [[Category: Thermobifida fusca]] | ||
| - | [[Category: Bottomley | + | [[Category: Bottomley SP]] |
| - | [[Category: Cabrita | + | [[Category: Cabrita LD]] |
| - | [[Category: Irving | + | [[Category: Irving JA]] |
| - | [[Category: Pike | + | [[Category: Pike RN]] |
| - | [[Category: Rossjohn | + | [[Category: Rossjohn J]] |
| - | [[Category: Whisstock | + | [[Category: Whisstock JC]] |
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Current revision
The X-ray crystal structure of a serpin from a thermophilic prokaryote
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