6s36
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of E. coli Adenylate kinase R119K mutant== | |
| + | <StructureSection load='6s36' size='340' side='right'caption='[[6s36]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6s36]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S36 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=6s36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s36 OCA], [http://pdbe.org/6s36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s36 RCSB], [http://www.ebi.ac.uk/pdbsum/6s36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s36 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A234NPI7_ECOLX A0A234NPI7_ECOLX]] 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.[HAMAP-Rule:MF_00235] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | As a key molecule in biology, adenosine triphosphate (ATP) has numerous crucial functions in, for instance, energetics, post-translational modifications, nucleotide biosynthesis, and cofactor metabolism. Here, we have discovered an intricate interplay between the enzyme adenylate kinase and its substrate ATP. The side chain of an arginine residue was found to be an efficient sensor of the aromatic moiety of ATP through the formation of a strong cation-pi interaction. In addition to recognition, the interaction was found to have dual functionality. First, it nucleates the activating conformational transition of the ATP binding domain and also affects the specificity in the distant AMP binding domain. In light of the functional consequences resulting from the cation-pi interaction, it is possible that the mode of ATP recognition may be a useful tool in enzyme design. | ||
| - | + | Nucleation of an Activating Conformational Change by a Cation-pi Interaction.,Rogne P, Andersson D, Grundstrom C, Sauer-Eriksson E, Linusson A, Wolf-Watz M Biochemistry. 2019 Jul 29. doi: 10.1021/acs.biochem.9b00538. PMID:31339702<ref>PMID:31339702</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6s36" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Adenylate kinase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Grundstrom, C]] | ||
| + | [[Category: Rogne, P]] | ||
| + | [[Category: Sauer-Eriksson, A E]] | ||
| + | [[Category: Wolf-Watz, M]] | ||
| + | [[Category: R119k variant]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:07, 7 August 2019
Crystal structure of E. coli Adenylate kinase R119K mutant
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