View source for 5jda


==Bacillus cereus CotH kinase plus Mg2+/AMP==
<StructureSection load='5jda' size='340' side='right'caption='[[5jda]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jda]] 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=5JDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JDA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.401&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jda OCA], [https://pdbe.org/5jda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jda RCSB], [https://www.ebi.ac.uk/pdbsum/5jda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jda ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q739M5_BACC1 Q739M5_BACC1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jda" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus cereus ATCC 10987]]
[[Category: Large Structures]]
[[Category: Sreelatha A]]
[[Category: Tagliabracci VS]]
[[Category: Tomchick DR]]