1bdj
From Proteopedia
(Difference between revisions)
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| - | + | ==COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY== | |
| - | + | <StructureSection load='1bdj' size='340' side='right' caption='[[1bdj]], [[Resolution|resolution]] 2.68Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[1bdj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BDJ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <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=1bdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bdj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bdj RCSB], [http://www.ebi.ac.uk/pdbsum/1bdj PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/1bdj_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three-dimensional structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3% at 2.68 A resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY. | ||
| - | + | Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY.,Kato M, Shimizu T, Mizuno T, Hakoshima T Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1257-63. PMID:10393292<ref>PMID:10393292</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
==See Also== | ==See Also== | ||
*[[Chemotaxis protein|Chemotaxis protein]] | *[[Chemotaxis protein|Chemotaxis protein]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Hakoshima, T.]] | [[Category: Hakoshima, T.]] | ||
Revision as of 04:15, 3 October 2014
COMPLEX STRUCTURE OF HPT DOMAIN AND CHEY
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