6fh3

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m (Protected "6fh3" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6fh3 is ON HOLD
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==Protein arginine kinase McsB in the pArg-bound state==
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<StructureSection load='6fh3' size='340' side='right' caption='[[6fh3]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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Authors: Suskiewicz, M.J., Heuck, A., Vu, L.D., Clausen, T.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6fh3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FH3 FirstGlance]. <br>
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Description: Protein arginine kinase McsB in the pArg-bound state
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=RPI:PHOSPHO-ARGININE'>RPI</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fh1|6fh1]], [[6fh2|6fh2]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_arginine_kinase Protein arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.14.1 2.7.14.1] </span></td></tr>
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<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=6fh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fh3 OCA], [http://pdbe.org/6fh3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fh3 RCSB], [http://www.ebi.ac.uk/pdbsum/6fh3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fh3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MCSB_GEOSE MCSB_GEOSE]] Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Acts exclusively on Arg residues, since it cannot phosphorylate Tyr, Ser, Thr, His, Asp and Lys.<ref>PMID:19498169</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Protein arginine kinase]]
[[Category: Clausen, T]]
[[Category: Clausen, T]]
[[Category: Heuck, A]]
[[Category: Heuck, A]]
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[[Category: Suskiewicz, M.J]]
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[[Category: Suskiewicz, M J]]
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[[Category: Vu, L.D]]
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[[Category: Vu, L D]]
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[[Category: Phospho-binding domain]]
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[[Category: Protein arginine phosphorylation]]
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[[Category: Protein kinase]]
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[[Category: Signaling protein]]

Revision as of 15:18, 27 February 2019

Protein arginine kinase McsB in the pArg-bound state

6fh3, resolution 1.85Å

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