3dms
From Proteopedia
(Difference between revisions)
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| - | + | ==1.65A crystal structure of isocitrate dehydrogenase from Burkholderia pseudomallei== | |
| - | ===1. | + | <StructureSection load='3dms' size='340' side='right' caption='[[3dms]], [[Resolution|resolution]] 1.65Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3dms]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DMS FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">icd, BPSL0896 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 Burkholderia pseudomallei])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </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=3dms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dms OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dms RCSB], [http://www.ebi.ac.uk/pdbsum/3dms PDBsum], [http://www.topsan.org/Proteins/SSGCID/3dms TOPSAN]</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/dm/3dms_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 == | ||
| + | Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhibits the necessary structural elements required for AceK recognition. Kinetic analyses provided further confirmation that Bp-ICDH is a substrate for AceK. We conclude that the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria. | ||
| - | + | Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.,Yates SP, Edwards TE, Bryan CM, Stein AJ, Van Voorhis WC, Myler PJ, Stewart LJ, Zheng J, Jia Z Biochemistry. 2011 Sep 27;50(38):8103-6. Epub 2011 Sep 2. PMID:21870819<ref>PMID:21870819</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[Ferguson sandbox 1|Ferguson sandbox 1]] | ||
*[[Isocitrate dehydrogenase|Isocitrate dehydrogenase]] | *[[Isocitrate dehydrogenase|Isocitrate dehydrogenase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Burkholderia pseudomallei]] | [[Category: Burkholderia pseudomallei]] | ||
| - | [[Category: | + | [[Category: Structural genomic]] |
[[Category: Burkholderia]] | [[Category: Burkholderia]] | ||
[[Category: Dehydrogenase]] | [[Category: Dehydrogenase]] | ||
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[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Pseudomallei]] | [[Category: Pseudomallei]] | ||
| - | [[Category: Seattle structural genomics center for infectious disease]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Tricarboxylic acid cycle]] | [[Category: Tricarboxylic acid cycle]] | ||
Revision as of 17:43, 21 December 2014
1.65A crystal structure of isocitrate dehydrogenase from Burkholderia pseudomallei
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