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6mel
From Proteopedia
(Difference between revisions)
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==Succinyl-CoA synthase from Campylobacter jejuni== | ==Succinyl-CoA synthase from Campylobacter jejuni== | ||
| - | <StructureSection load='6mel' size='340' side='right' caption='[[6mel]], [[Resolution|resolution]] 2.06Å' scene=''> | + | <StructureSection load='6mel' size='340' side='right'caption='[[6mel]], [[Resolution|resolution]] 2.06Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6mel]] is a 2 chain structure. 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> | + | <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> |
</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> | </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> | ||
| + | <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> | ||
<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> | <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> | ||
<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> | <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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== Function == | == Function == | ||
[[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. | [[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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| + | ==See Also== | ||
| + | *[[Succinyl-CoA synthetase|Succinyl-CoA synthetase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Campylobacter fetus subsp. jejuni smibert 1974]] | ||
| + | [[Category: Camjr]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Jedrzejczak, R]] | [[Category: Jedrzejczak, R]] | ||
Revision as of 10:54, 18 December 2019
Succinyl-CoA synthase from Campylobacter jejuni
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