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1scu
From Proteopedia
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|PDB= 1scu |SIZE=350|CAPTION= <scene name='initialview01'>1scu</scene>, resolution 2.5Å | |PDB= 1scu |SIZE=350|CAPTION= <scene name='initialview01'>1scu</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene> | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene>, <scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1scu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scu OCA], [http://www.ebi.ac.uk/pdbsum/1scu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1scu RCSB]</span> | ||
}} | }} | ||
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[[Category: James, M N.G.]] | [[Category: James, M N.G.]] | ||
[[Category: Wolodko, W T.]] | [[Category: Wolodko, W T.]] | ||
| - | [[Category: COA]] | ||
| - | [[Category: PHS]] | ||
[[Category: ligase (atp-binding)]] | [[Category: ligase (atp-binding)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:40:19 2008'' |
Revision as of 20:40, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Succinate--CoA ligase (ADP-forming), with EC number 6.2.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION
Overview
The x-ray crystal structure of succinyl-CoA synthetase (SCS) from Escherichia coli has been determined by the method of multiple isomorphous replacement to a resolution of 2.5 A. Crystals of SCS are tetragonal with a space group of P4(3)22 and unit cell dimensions of a = b = 98.47 A and c = 400.6 A. One molecule of SCS (142 kDa) is contained in the asymmetric unit. The current model has been refined to a conventional R factor of 21.6% with root mean square deviations from ideal stereochemistry of 0.022 A for bond lengths and 3.25 degrees for bond angles. The quaternary organization of the E. coli enzyme is an alpha 2 beta 2 heterotetramer. In this tetramer, the alpha-subunits interact only with the beta-subunits, whereas the beta-subunits interact to form the dimer of alpha beta-dimers. The two active site pockets are located at regions of contact between alpha- and beta-subunits. One molecule of coenzyme A is bound to each alpha-subunit at a typical nucleotide-binding motif, and His-246 of each alpha-subunit is phosphorylated. This phosphohistidine, a catalytic intermediate, is stabilized by two helix dipoles (the "power" helices), one from each of the two subunit types. A short segment of the beta-subunit from one alpha beta-dimer is in close proximity to the CoA-binding site of the other alpha beta-dimer, providing a possible rationale for the overall tetrameric structure.
About this Structure
1SCU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution., Wolodko WT, Fraser ME, James MN, Bridger WA, J Biol Chem. 1994 Apr 8;269(14):10883-90. PMID:8144675
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