6bms: Difference between revisions

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==Palmitoyltransferase structure==
==Palmitoyltransferase structure==
<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. 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='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='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='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>
<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>
</table>
</table>
== Function ==
[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>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Protein S-acyltransferase]]
[[Category: Danio rerio]]
[[Category: Kumar, P]]
[[Category: Large Structures]]
[[Category: Rajashankar, K]]
[[Category: Kumar P]]
[[Category: Membrane bound enzyme]]
[[Category: Rajashankar K]]
[[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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