3gmt
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of adenylate kinase from burkholderia pseudomallei== | |
- | === | + | <StructureSection load='3gmt' size='340' side='right' caption='[[3gmt]], [[Resolution|resolution]] 2.10Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3gmt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GMT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GMT FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adk, BURPS1710b_1080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 Burkholderia pseudomallei 1710b])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </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=3gmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gmt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gmt RCSB], [http://www.ebi.ac.uk/pdbsum/3gmt 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/gm/3gmt_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 == | ||
+ | In all organisms adenylate kinases (Adks) play a vital role in cellular energy metabolism and nucleic acid synthesis. Due to differences in catalytic properties between the Adks found in prokaryotes and in the cytoplasm of eukaryotes, there is interest in targeting this enzyme for new drug therapies against infectious bacterial agents. Here we report the 2.1A resolution crystal structure for the 220-residue Adk from Burkholderia pseudomallei (BpAdk), the etiological agent responsible for the infectious disease melioidosis. The general structure of apo BpAdk is similar to other Adk structures, composed of a CORE subdomain with peripheral ATP-binding (ATP(bd)) and LID subdomains. The two molecules in the asymmetric unit have significantly different conformations, with a backbone RMSD of 1.46 A. These two BpAdk conformations may represent 'open' Adk sub-states along the preferential pathway to the 'closed' substrate-bound state. | ||
- | + | Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): profound asymmetry in the crystal structure of the 'open' state.,Buchko GW, Robinson H, Abendroth J, Staker BL, Myler PJ Biochem Biophys Res Commun. 2010 Apr 16;394(4):1012-7. Epub 2010 Mar 21. PMID:20331978<ref>PMID:20331978</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
==See Also== | ==See Also== | ||
*[[Adenylate kinase|Adenylate kinase]] | *[[Adenylate kinase|Adenylate kinase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Adenylate kinase]] | [[Category: Adenylate kinase]] | ||
[[Category: Burkholderia pseudomallei 1710b]] | [[Category: Burkholderia pseudomallei 1710b]] | ||
- | [[Category: Abendroth, J | + | [[Category: Abendroth, J]] |
- | [[Category: Buchko, G W | + | [[Category: Buchko, G W]] |
- | [[Category: Hewitt, S N | + | [[Category: Hewitt, S N]] |
- | [[Category: Myler, P J | + | [[Category: Myler, P J]] |
- | [[Category: Napuli, A J | + | [[Category: Napuli, A J]] |
- | [[Category: Robinson, H | + | [[Category: Robinson, H]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: Stacy, R | + | [[Category: Stacy, R]] |
- | [[Category: Staker, B L | + | [[Category: Staker, B L]] |
- | [[Category: Stewart, L | + | [[Category: Stewart, L]] |
- | [[Category: Voorhis, W Van | + | [[Category: Voorhis, W Van]] |
- | + | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Burkholderia pseudomallei]] | [[Category: Burkholderia pseudomallei]] | ||
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[[Category: Nucleotide biosynthesis]] | [[Category: Nucleotide biosynthesis]] | ||
[[Category: Nucleotide-binding]] | [[Category: Nucleotide-binding]] | ||
- | [[Category: Seattle structural genomics center for infectious disease]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||
- | [[Category: Structural genomic]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 15:35, 18 December 2014
Crystal structure of adenylate kinase from burkholderia pseudomallei
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Categories: Adenylate kinase | Burkholderia pseudomallei 1710b | Abendroth, J | Buchko, G W | Hewitt, S N | Myler, P J | Napuli, A J | Robinson, H | Structural genomic | Stacy, R | Staker, B L | Stewart, L | Voorhis, W Van | Atp-binding | Burkholderia pseudomallei | Kinase | Nucleotide biosynthesis | Nucleotide-binding | Ssgcid | Transferase