3ju5
From Proteopedia
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- | + | ==Crystal Structure of Dimeric Arginine Kinase at 1.75-A Resolution== | |
- | + | <StructureSection load='3ju5' size='340' side='right' caption='[[3ju5]], [[Resolution|resolution]] 1.75Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3ju5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Apostichopus_japonicus Apostichopus japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JU5 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ju6|3ju6]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=307972 Apostichopus japonicus])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] </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=3ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ju5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ju5 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/ju/3ju5_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 == | ||
+ | Phosphagen kinase (PK) family members catalyze the reversible phosphoryl transfer between phosphagen and ADP to reserve or release energy in cell energy metabolism. The structures of classic quaternary complexes of dimeric creatine kinase (CK) revealed asymmetric ligand binding states of two protomers, but the significance and mechanism remain unclear. To understand this negative cooperativity further, we determined the first structure of dimeric arginine kinase (dAK), another PK family member, at 1.75 A, as well as the structure of its ternary complex with AMPPNP and arginine. Further structural analysis shows that the ligand-free protomer in a ligand-bound dimer opens more widely than the protomers in a ligand-free dimer, which leads to three different states of a dAK protomer. The unexpected allostery of the ligand-free protomer in a ligand-bound dimer should be relayed from the ligand-binding-induced allostery of its adjacent protomer. Mutations that weaken the interprotomer connections dramatically reduced the catalytic activities of dAK, indicating the importance of the allosteric propagation mediated by the homodimer interface. These results suggest a reciprocating mechanism of dimeric PK, which is shared by other ATP related oligomeric enzymes, e.g., ATP synthase. | ||
- | + | Structural basis for a reciprocating mechanism of negative cooperativity in dimeric phosphagen kinase activity.,Wu X, Ye S, Guo S, Yan W, Bartlam M, Rao Z FASEB J. 2010 Jan;24(1):242-52. Epub 2009 Sep 25. PMID:19783784<ref>PMID:19783784</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Apostichopus japonicus]] | [[Category: Apostichopus japonicus]] | ||
[[Category: Arginine kinase]] | [[Category: Arginine kinase]] | ||
- | [[Category: Bartlam, M | + | [[Category: Bartlam, M]] |
- | [[Category: Guo, S | + | [[Category: Guo, S]] |
- | [[Category: Rao, Z | + | [[Category: Rao, Z]] |
- | [[Category: Wu, X | + | [[Category: Wu, X]] |
- | [[Category: Yan, W | + | [[Category: Yan, W]] |
- | [[Category: Ye, S | + | [[Category: Ye, S]] |
- | + | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Kinase]] | [[Category: Kinase]] |
Revision as of 16:10, 18 December 2014
Crystal Structure of Dimeric Arginine Kinase at 1.75-A Resolution
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