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New page: '''Unreleased structure''' The entry 6mel is ON HOLD Authors: Osipiuk, J., Maltseva, N., Jedrzejczak, R., Satchell, K.J.F., Joachimiak, A., Center for Structural Genomics of Infectious ... |
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The | ==Succinyl-CoA synthase from Campylobacter jejuni== | ||
<StructureSection load='6mel' size='340' side='right'caption='[[6mel]], [[Resolution|resolution]] 2.06Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mel]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] and [https://en.wikipedia.org/wiki/Campylobacter_jejuni_RM1221 Campylobacter jejuni RM1221]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MEL 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]] 2.06Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=6mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mel OCA], [https://pdbe.org/6mel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mel RCSB], [https://www.ebi.ac.uk/pdbsum/6mel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mel ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0PAY2_CAMJE Q0PAY2_CAMJE] Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.[HAMAP-Rule:MF_01988][RuleBase:RU000699] | |||
==See Also== | |||
*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Campylobacter jejuni]] | ||
[[Category: | [[Category: Campylobacter jejuni RM1221]] | ||
[[Category: Joachimiak | [[Category: Large Structures]] | ||
[[Category: | [[Category: Jedrzejczak R]] | ||
[[Category: Osipiuk | [[Category: Joachimiak A]] | ||
[[Category: | [[Category: Maltseva N]] | ||
[[Category: Osipiuk J]] | |||
[[Category: Satchell KJF]] | |||
Latest revision as of 09:30, 11 October 2023
Succinyl-CoA synthase from Campylobacter jejuniSuccinyl-CoA synthase from Campylobacter jejuni
Structural highlights
FunctionQ0PAY2_CAMJE Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.[HAMAP-Rule:MF_01988][RuleBase:RU000699] See Also |
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