4xx0: Difference between revisions
New page: '''Unreleased structure''' The entry 4xx0 is ON HOLD Authors: Fraser, M.E., Huang, J., Malhi, M. Description: CoA bound to pig GTP-specific succinyl-CoA synthetase [[Category: Unreleas... |
No edit summary |
||
(7 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
The | ==CoA bound to pig GTP-specific succinyl-CoA synthetase== | ||
<StructureSection load='4xx0' size='340' side='right'caption='[[4xx0]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xx0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XX0 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xx0 OCA], [https://pdbe.org/4xx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xx0 RCSB], [https://www.ebi.ac.uk/pdbsum/4xx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xx0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SUCA_PIG SUCA_PIG] Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pig GTP-specific succinyl-CoA synthetase is an alphabeta-heterodimer. The crystal structure of the complex with the substrate CoA was determined at 2.1 A resolution. The structure shows CoA bound to the amino-terminal domain of the alpha-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides. | |||
Structure of GTP-specific succinyl-CoA synthetase in complex with CoA.,Huang J, Malhi M, Deneke J, Fraser ME Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1067-71. doi:, 10.1107/S2053230X15011188. Epub 2015 Jul 29. PMID:26249701<ref>PMID:26249701</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4xx0" style="background-color:#fffaf0;"></div> | ||
[[Category: Fraser | |||
[[Category: Malhi | ==See Also== | ||
*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | |||
[[Category: Fraser ME]] | |||
[[Category: Huang J]] | |||
[[Category: Malhi M]] |
Latest revision as of 03:55, 28 December 2023
CoA bound to pig GTP-specific succinyl-CoA synthetaseCoA bound to pig GTP-specific succinyl-CoA synthetase
Structural highlights
FunctionSUCA_PIG Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). Publication Abstract from PubMedPig GTP-specific succinyl-CoA synthetase is an alphabeta-heterodimer. The crystal structure of the complex with the substrate CoA was determined at 2.1 A resolution. The structure shows CoA bound to the amino-terminal domain of the alpha-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides. Structure of GTP-specific succinyl-CoA synthetase in complex with CoA.,Huang J, Malhi M, Deneke J, Fraser ME Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1067-71. doi:, 10.1107/S2053230X15011188. Epub 2015 Jul 29. PMID:26249701[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|