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5jd9

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==Bacillus cereus CotH kinase==
==Bacillus cereus CotH kinase==
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<StructureSection load='5jd9' size='340' side='right' caption='[[5jd9]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
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<StructureSection load='5jd9' size='340' side='right'caption='[[5jd9]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jd9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JD9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jd9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_10987 Bacillus cereus ATCC 10987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JD9 FirstGlance]. <br>
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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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63&#8491;</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=5jd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jd9 OCA], [http://pdbe.org/5jd9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jd9 RCSB], [http://www.ebi.ac.uk/pdbsum/5jd9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jd9 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jd9 OCA], [https://pdbe.org/5jd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jd9 RCSB], [https://www.ebi.ac.uk/pdbsum/5jd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jd9 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q739M5_BACC1 Q739M5_BACC1]
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The modification of proteins by phosphorylation occurs in all life forms and is catalyzed by a large superfamily of enzymes known as protein kinases. We recently discovered a family of secretory pathway kinases that phosphorylate extracellular proteins. One member, family with sequence similarity 20C (Fam20C), is the physiological Golgi casein kinase. While examining distantly related protein sequences, we observed low levels of identity between the spore coat protein H (CotH), and the Fam20C-related secretory pathway kinases. CotH is a component of the spore in many bacterial and eukaryotic species, and is required for efficient germination of spores in Bacillus subtilis; however, the mechanism by which CotH affects germination is unclear. Here, we show that CotH is a protein kinase. The crystal structure of CotH reveals an atypical protein kinase-like fold with a unique mode of ATP binding. Examination of the genes neighboring cotH in B. subtilis led us to identify two spore coat proteins, CotB and CotG, as CotH substrates. Furthermore, we show that CotH-dependent phosphorylation of CotB and CotG is required for the efficient germination of B. subtilis spores. Collectively, our results define a family of atypical protein kinases and reveal an unexpected role for protein phosphorylation in spore biology.
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Phosphorylation of spore coat proteins by a family of atypical protein kinases.,Nguyen KB, Sreelatha A, Durrant ES, Lopez-Garrido J, Muszewska A, Dudkiewicz M, Grynberg M, Yee S, Pogliano K, Tomchick DR, Pawlowski K, Dixon JE, Tagliabracci VS Proc Natl Acad Sci U S A. 2016 May 16. pii: 201605917. PMID:27185916<ref>PMID:27185916</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5jd9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Sreelatha, A]]
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[[Category: Bacillus cereus ATCC 10987]]
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[[Category: Tagliabracci, V S]]
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[[Category: Large Structures]]
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[[Category: Tomchick, D R]]
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[[Category: Sreelatha A]]
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[[Category: Atypical kinase fold]]
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[[Category: Tagliabracci VS]]
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[[Category: Structural protein]]
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[[Category: Tomchick DR]]

Current revision

Bacillus cereus CotH kinase

PDB ID 5jd9

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