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6bmm

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'''Unreleased structure'''
 
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The entry 6bmm is ON HOLD until Paper Publication
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==Structure of human DHHC20 palmitoyltransferase, space group P21==
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<StructureSection load='6bmm' size='340' side='right' caption='[[6bmm]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6bmm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BMM 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=DYD:(2S,5S)-hexane-2,5-diol'>DYD</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZDHHC20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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_S-acyltransferase Protein S-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.225 2.3.1.225] </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=6bmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bmm OCA], [http://pdbe.org/6bmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bmm RCSB], [http://www.ebi.ac.uk/pdbsum/6bmm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bmm ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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DHHC (Asp-His-His-Cys) palmitoyltransferases are eukaryotic integral membrane enzymes that catalyze protein palmitoylation, which is important in a range of physiological processes, including small guanosine triphosphatase (GTPase) signaling, cell adhesion, and neuronal receptor scaffolding. We present crystal structures of two DHHC palmitoyltransferases and a covalent intermediate mimic. The active site resides at the membrane-cytosol interface, which allows the enzyme to catalyze thioester-exchange chemistry by using fatty acyl-coenzyme A and explains why membrane-proximal cysteines are candidates for palmitoylation. The acyl chain binds in a cavity formed by the transmembrane domain. We propose a mechanism for acyl chain-length selectivity in DHHC enzymes on the basis of cavity mutants with preferences for shorter and longer acyl chains.
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Authors: Lee, C.-J.
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Fatty acyl recognition and transfer by an integral membrane S-acyltransferase.,Rana MS, Kumar P, Lee CJ, Verardi R, Rajashankar KR, Banerjee A Science. 2018 Jan 12;359(6372). pii: 359/6372/eaao6326. doi:, 10.1126/science.aao6326. PMID:29326245<ref>PMID:29326245</ref>
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Description: lipid enzyme p21
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Lee, C.-J]]
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<div class="pdbe-citations 6bmm" style="background-color:#fffaf0;"></div>
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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: Human]]
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[[Category: Protein S-acyltransferase]]
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[[Category: Banerjee, A]]
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[[Category: Lee, C J]]
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[[Category: Rana, M S]]
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[[Category: Acyl]]
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[[Category: Dhhc]]
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[[Category: Lipid]]
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[[Category: Palmitoyltransferase]]
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[[Category: Transferase]]

Current revision

Structure of human DHHC20 palmitoyltransferase, space group P21

6bmm, resolution 2.35Å

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