4x3f
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of the intracellular domain of the M. tuberculosis Ser/Thr kinase PknA== |
+ | <StructureSection load='4x3f' size='340' side='right' caption='[[4x3f]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4x3f]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X3F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X3F FirstGlance]. <br> | ||
+ | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4x3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x3f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x3f RCSB], [http://www.ebi.ac.uk/pdbsum/4x3f PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/PKNA_MYCTU PKNA_MYCTU]] Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as FtsZ, Wag31, GlmU, FhaB, PstP, EmbR and Rv1422. Shows a strong preference for Thr versus Ser as the phosphoacceptor.<ref>PMID:15985609</ref> <ref>PMID:16817899</ref> <ref>PMID:19121323</ref> <ref>PMID:20066037</ref> <ref>PMID:21190553</ref> <ref>PMID:21423706</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Signal transduction mediated by Ser/Thr phosphorylation in Mycobacterium tuberculosis has been intensively studied in the last years, as its genome harbors eleven genes coding for eukaryotic-like Ser/Thr kinases. Here we describe the crystal structure and the autophosphorylation sites of the catalytic domain of PknA, one of two protein kinases essential for pathogen's survival. The structure of the ligand-free kinase domain shows an auto-inhibited conformation similar to that observed in human Tyr kinases of the Src-family. These results reinforce the high conservation of structural hallmarks and regulation mechanisms between prokaryotic and eukaryotic protein kinases. This article is protected by copyright. All rights reserved. | ||
- | The | + | The crystal structure of the catalytic domain of the Ser/Thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.,Wagner T, Alexandre M, Duran R, Barilone N, Wehenkel A, Alzari PM, Bellinzoni M Proteins. 2015 Jan 13. doi: 10.1002/prot.24754. PMID:25586004<ref>PMID:25586004</ref> |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Non-specific serine/threonine protein kinase]] | ||
+ | [[Category: Alzari, P M]] | ||
+ | [[Category: Bellinzoni, M]] | ||
[[Category: Wagner, T]] | [[Category: Wagner, T]] | ||
- | [[Category: Alzari, P.M]] | ||
- | [[Category: Bellinzoni, M]] | ||
[[Category: Wehenkel, A]] | [[Category: Wehenkel, A]] | ||
+ | [[Category: Autoinhibition]] | ||
+ | [[Category: Kinase]] | ||
+ | [[Category: Phosphorylation]] | ||
+ | [[Category: Transferase]] |
Revision as of 16:45, 21 January 2015
Crystal structure of the intracellular domain of the M. tuberculosis Ser/Thr kinase PknA
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