6mel
From Proteopedia
(Difference between revisions)
(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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| - | '''Unreleased structure''' | ||
| - | + | ==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]] | ||
Current revision
Succinyl-CoA synthase from Campylobacter jejuni
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