1iuk: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1iuk]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IUK FirstGlance]. <br>
<table><tr><td colspan='2'>[[1iuk]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IUK FirstGlance]. <br>
</td></tr><tr><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">[[1iul|1iul]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iuk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iuk RCSB], [http://www.ebi.ac.uk/pdbsum/1iuk PDBsum], [http://www.topsan.org/Proteins/RSGI/1iuk TOPSAN]</span></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=1iuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iuk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iuk RCSB], [http://www.ebi.ac.uk/pdbsum/1iuk PDBsum], [http://www.topsan.org/Proteins/RSGI/1iuk TOPSAN]</span></td></tr>
<table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
[[Category: Kuramitsu, S.]]
[[Category: Kuramitsu, S]]
[[Category: Park, S Y.]]
[[Category: Park, S Y]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Structural genomic]]
[[Category: Shirouzu, M.]]
[[Category: Shirouzu, M]]
[[Category: Tame, J R.]]
[[Category: Tame, J R]]
[[Category: Wada, T.]]
[[Category: Wada, T]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Unknown function]]
[[Category: Unknown function]]

Revision as of 17:14, 25 December 2014

The structure of native ID.343 from Thermus thermophilusThe structure of native ID.343 from Thermus thermophilus

Structural highlights

1iuk is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum, TOPSAN

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 PubMed

TT1466 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

  1. Wada T, Shirouzu M, Terada T, Ishizuka Y, Matsuda T, Kigawa T, Kuramitsu S, Park SY, Tame JR, Yokoyama S. Structure of a conserved CoA-binding protein synthesized by a cell-free system. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1213-8. Epub 2003, Jun 27. PMID:12832765

1iuk, resolution 1.70Å

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OCA