3gmt
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3gmt is ON HOLD Authors: Ssgcid, Seattle Structural Genomics Center for Infectious Disease (SSGCID) Description: Crystal structure of adenylate kin...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3GMT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gmt OCA], [https://pdbe.org/3gmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gmt RCSB], [https://www.ebi.ac.uk/pdbsum/3gmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gmt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KAD_BURP1 KAD_BURP1] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity). | ||
| + | == 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/initialview03.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/main_output.php?pdb_ID=3gmt 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> | ||
| + | <div class="pdbe-citations 3gmt" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Burkholderia pseudomallei 1710b]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Abendroth J]] | ||
| + | [[Category: Buchko GW]] | ||
| + | [[Category: Hewitt SN]] | ||
| + | [[Category: Myler PJ]] | ||
| + | [[Category: Napuli AJ]] | ||
| + | [[Category: Robinson H]] | ||
| + | [[Category: Stacy R]] | ||
| + | [[Category: Staker BL]] | ||
| + | [[Category: Stewart L]] | ||
| + | [[Category: Van Voorhis W]] | ||
Current revision
Crystal structure of adenylate kinase from burkholderia pseudomallei
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