1mp9: Difference between revisions
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<StructureSection load='1mp9' size='340' side='right' caption='[[1mp9]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1mp9' size='340' side='right' caption='[[1mp9]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mp9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1mp9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MP9 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=1mp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mp9 RCSB], [http://www.ebi.ac.uk/pdbsum/1mp9 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=1mp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp9 OCA], [http://pdbe.org/1mp9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mp9 RCSB], [http://www.ebi.ac.uk/pdbsum/1mp9 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 1mp9" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 33909]] | ||
[[Category: Clowney, L]] | [[Category: Clowney, L]] | ||
[[Category: Katsuya, Y]] | [[Category: Katsuya, Y]] | ||
Revision as of 08:56, 11 September 2015
TBP from a mesothermophilic archaeon, Sulfolobus acidocaldariusTBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius
Structural highlights
Function[TBP_SULAC] General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity). 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 PubMedThe crystal structure of TATA binding protein (TBP) from a mesothermophilic archaeon, Sulfolobus acidocaldarius, has been determined at a resolution of 2.0 A with an R factor of 20.9%. By comparing this structure with the structures of TBPs from a hyperthermophilic archaeon and mesophilic eukaryotes, as well as by comparing amino acid sequences of TBPs from archaea, covering a wide range of optimum growth temperatures, two significant determinants of the stability of TBP have been identified: increasing the interior hydrophobicity by interaction between three residues, Val, Leu, and Ile, with further differentiation of the surface, and increasing its hydrophilicity and raising the cost of unfolding. These findings suggest directions along which the stability of TBP can be engineered. Origins of protein stability revealed by comparing crystal structures of TATA binding proteins.,Koike H, Kawashima-Ohya Y, Yamasaki T, Clowney L, Katsuya Y, Suzuki M Structure. 2004 Jan;12(1):157-68. PMID:14725775[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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