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2nua
From Proteopedia
(Difference between revisions)
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==C123aV Mutant of E. coli Succinyl-CoA Synthetase== | ==C123aV Mutant of E. coli Succinyl-CoA Synthetase== | ||
| - | <StructureSection load='2nua' size='340' side='right' caption='[[2nua]], [[Resolution|resolution]] 2.95Å' scene=''> | + | <StructureSection load='2nua' size='340' side='right'caption='[[2nua]], [[Resolution|resolution]] 2.95Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2nua]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2nua]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NUA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2scu|2scu]], [[1jkj|1jkj]], [[1jll|1jll]], [[2nu6|2nu6]], [[2nu7|2nu7]], [[2nu8|2nu8]], [[2nu9|2nu9]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2scu|2scu]], [[1jkj|1jkj]], [[1jll|1jll]], [[2nu6|2nu6]], [[2nu7|2nu7]], [[2nu8|2nu8]], [[2nu9|2nu9]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sucD ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sucD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), sucC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate--CoA_ligase_(ADP-forming) Succinate--CoA ligase (ADP-forming)], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nua OCA], [https://pdbe.org/2nua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nua RCSB], [https://www.ebi.ac.uk/pdbsum/2nua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nua ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/SUCD_ECOLI SUCD_ECOLI]] During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. The alpha-subunit binds CoA, as well as ATP and catalyzes phosphoryl transfer to one of its histidine residues. The complete active site is probably located in the region of alpha-beta contact. [[https://www.uniprot.org/uniprot/SUCC_ECOLI SUCC_ECOLI]] During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. The beta-subunit contains the attachment sites for succinate. The complete active site is probably located in the region of alpha-beta contact. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Succinyl-CoA synthetase|Succinyl-CoA synthetase]] | + | *[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Fraser, M E]] | [[Category: Fraser, M E]] | ||
[[Category: Atp-grasp fold]] | [[Category: Atp-grasp fold]] | ||
Revision as of 15:51, 8 June 2021
C123aV Mutant of E. coli Succinyl-CoA Synthetase
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