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6mel

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Current revision (06:30, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6mel' size='340' side='right'caption='[[6mel]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
<StructureSection load='6mel' size='340' side='right'caption='[[6mel]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6mel]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974] and [http://en.wikipedia.org/wiki/Camjr Camjr]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MEL FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDV82_04720, DDV86_02895 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 "Campylobacter fetus subsp. jejuni" Smibert 1974]), sucC, CJE0637 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195099 CAMJR])</td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate--CoA_ligase_(ADP-forming) Succinate--CoA ligase (ADP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.5 6.2.1.5] </span></td></tr>
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<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>
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<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=6mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mel OCA], [http://pdbe.org/6mel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mel RCSB], [http://www.ebi.ac.uk/pdbsum/6mel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mel ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SUCC_CAMJR SUCC_CAMJR]] 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 beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
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[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==
==See Also==
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*[[Succinyl-CoA synthetase|Succinyl-CoA synthetase]]
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*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Campylobacter fetus subsp. jejuni smibert 1974]]
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[[Category: Campylobacter jejuni]]
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[[Category: Camjr]]
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[[Category: Campylobacter jejuni RM1221]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Jedrzejczak R]]
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[[Category: Jedrzejczak, R]]
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[[Category: Joachimiak A]]
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[[Category: Joachimiak, A]]
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[[Category: Maltseva N]]
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[[Category: Maltseva, N]]
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[[Category: Osipiuk J]]
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[[Category: Osipiuk, J]]
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[[Category: Satchell KJF]]
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[[Category: Satchell, K J.F]]
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[[Category: Cpx_90676_90715]]
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[[Category: Csgid]]
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[[Category: Idp90676]]
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[[Category: Idp90715]]
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[[Category: Ligase]]
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[[Category: Succinyl-coa synthase]]
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Current revision

Succinyl-CoA synthase from Campylobacter jejuni

PDB ID 6mel

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