1iuk: Difference between revisions
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<StructureSection load='1iuk' size='340' side='right'caption='[[1iuk]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1iuk' size='340' side='right'caption='[[1iuk]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iuk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1iuk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUK FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iul|1iul]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iul|1iul]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iuk OCA], [https://pdbe.org/1iuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iuk RCSB], [https://www.ebi.ac.uk/pdbsum/1iuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iuk ProSAT], [https://www.topsan.org/Proteins/RSGI/1iuk TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == |
Revision as of 10:14, 14 April 2021
The structure of native ID.343 from Thermus thermophilusThe structure of native ID.343 from Thermus thermophilus
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 PubMedTT1466 is a hypothetical protein from the extremely thermophilic bacterium Thermus thermophilus HB8 and is highly conserved in bacteria and archaea. The selenomethionyl protein was synthesized by a cell-free system and the crystal structure was determined at 2.0 A by MAD phasing. A native crystal was used for structure refinement to 1.7 A. The structure is highly homologous to that of the CoA-binding domain of the succinyl-CoA synthetase from Escherichia coli, despite the protein having only 14% sequence identity to this domain. An isothermal titration calorimetry experiment was performed to investigate whether TT1466 binds CoA and revealed high-affinity CoA binding of TT1466. Structure of a conserved CoA-binding protein synthesized by a cell-free system.,Wada T, Shirouzu M, Terada T, Ishizuka Y, Matsuda T, Kigawa T, Kuramitsu S, Park SY, Tame JR, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1213-8. Epub 2003, Jun 27. PMID:12832765[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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