6bms: Difference between revisions

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<StructureSection load='6bms' size='340' side='right'caption='[[6bms]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
<StructureSection load='6bms' size='340' side='right'caption='[[6bms]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6bms]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BMS FirstGlance]. <br>
<table><tr><td colspan='2'>[[6bms]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BMS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.441&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">zdhhc15b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bms OCA], [https://pdbe.org/6bms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bms RCSB], [https://www.ebi.ac.uk/pdbsum/6bms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bms ProSAT]</span></td></tr>
<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=6bms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bms OCA], [http://pdbe.org/6bms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bms RCSB], [http://www.ebi.ac.uk/pdbsum/6bms PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bms ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/ZH15B_DANRE ZH15B_DANRE] Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:29326245). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). May thereby regulate target proteins association and localization to membranes (By similarity). In the nervous system, probably catalyzes the palmitoylation of synaptic proteins and is involved in the differentiation of dopaminergic neurons and the development of the diencephalon (PubMed:26095893).[UniProtKB:Q8BGJ0][UniProtKB:Q96MV8]<ref>PMID:26095893</ref> <ref>PMID:29326245</ref>  
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bms" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Brachidanio rerio]]
[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein S-acyltransferase]]
[[Category: Kumar P]]
[[Category: Kumar, P]]
[[Category: Rajashankar K]]
[[Category: Rajashankar, K]]
[[Category: Membrane bound enzyme]]
[[Category: Membrane protein]]

Latest revision as of 17:22, 13 March 2024

Palmitoyltransferase structurePalmitoyltransferase structure

Structural highlights

6bms is a 2 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.441Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZH15B_DANRE Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:29326245). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). May thereby regulate target proteins association and localization to membranes (By similarity). In the nervous system, probably catalyzes the palmitoylation of synaptic proteins and is involved in the differentiation of dopaminergic neurons and the development of the diencephalon (PubMed:26095893).[UniProtKB:Q8BGJ0][UniProtKB:Q96MV8][1] [2]

References

  1. ↑ Wang F, Chen X, Shi W, Yao L, Gao M, Yang Y, Hao A. Zdhhc15b Regulates Differentiation of Diencephalic Dopaminergic Neurons in zebrafish. J Cell Biochem. 2015 Dec;116(12):2980-91. PMID:26095893 doi:10.1002/jcb.25256
  2. ↑ Rana MS, Kumar P, Lee CJ, Verardi R, Rajashankar KR, Banerjee A. Fatty acyl recognition and transfer by an integral membrane S-acyltransferase. Science. 2018 Jan 12;359(6372). pii: 359/6372/eaao6326. doi:, 10.1126/science.aao6326. PMID:29326245 doi:http://dx.doi.org/10.1126/science.aao6326

6bms, resolution 2.44Å

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