1mtp: Difference between revisions

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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]] 1.50&Aring;' scene=''>
<StructureSection load='1mtp' size='340' side='right'caption='[[1mtp]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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 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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mtp ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<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>
</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>
Line 16: Line 19:
</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].
</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.


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>
==See Also==
 
*[[Serpin 3D structures|Serpin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mtp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Thermonospora fusca henssen 1957]]
[[Category: Large Structures]]
[[Category: Bottomley, S P]]
[[Category: Thermobifida fusca]]
[[Category: Cabrita, L D]]
[[Category: Bottomley SP]]
[[Category: Irving, J A]]
[[Category: Cabrita LD]]
[[Category: Pike, R N]]
[[Category: Irving JA]]
[[Category: Rossjohn, J]]
[[Category: Pike RN]]
[[Category: Whisstock, J C]]
[[Category: Rossjohn J]]
[[Category: Protease inhibitor]]
[[Category: Whisstock JC]]
[[Category: Structural genomic]]

Latest revision as of 10:48, 14 February 2024

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

1mtp is a 2 chain structure with sequence from Thermobifida fusca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q47NK3_THEFY

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1mtp, resolution 1.50Å

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OCA
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