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5dzt

From Proteopedia

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<StructureSection load='5dzt' size='340' side='right'caption='[[5dzt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5dzt' size='340' side='right'caption='[[5dzt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dzt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DZT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dzt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DZT 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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ef0046, cylM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5dzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dzt OCA], [http://pdbe.org/5dzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dzt RCSB], [http://www.ebi.ac.uk/pdbsum/5dzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dzt ProSAT]</span></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=5dzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dzt OCA], [https://pdbe.org/5dzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dzt RCSB], [https://www.ebi.ac.uk/pdbsum/5dzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dzt 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/Q8KUA3_ENTFL Q8KUA3_ENTFL]
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The enterococcal cytolysin is a virulence factor consisting of two post-translationally modified peptides that synergistically kill human immune cells. Both peptides are made by CylM, a member of the LanM lanthipeptide synthetases. CylM catalyzes seven dehydrations of Ser and Thr residues and three cyclization reactions during the biosynthesis of the cytolysin large subunit. We present here the 2.2 A resolution structure of CylM, the first structural information on a LanM. Unexpectedly, the structure reveals that the dehydratase domain of CylM resembles the catalytic core of eukaryotic lipid kinases, despite the absence of clear sequence homology. The kinase and phosphate elimination active sites that affect net dehydration are immediately adjacent to each other. Characterization of mutants provided insights into the mechanism of the dehydration process. The structure is also of interest because of the interactions of human homologs of lanthipeptide cyclases with kinases such as mammalian target of rapamycin.
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The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold.,Dong SH, Tang W, Lukk T, Yu Y, Nair SK, van der Donk WA Elife. 2015 Jul 30;4. doi: 10.7554/eLife.07607. PMID:26226635<ref>PMID:26226635</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 5dzt" 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: Enterococcus proteiformis thiercelin and jouhaud 1903]]
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[[Category: Enterococcus faecalis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dong, S H]]
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[[Category: Dong SH]]
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[[Category: Lukk, T]]
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[[Category: Lukk T]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Cylm]]
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[[Category: Cytolysin]]
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[[Category: Kinase]]
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[[Category: Lanthipeptide synthetase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of class II lanthipeptide synthetase CylM in complex with AMP

PDB ID 5dzt

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