1scu
From Proteopedia
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'''THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION''' | '''THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION''' | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Succinate--CoA ligase (ADP-forming)]] | ||
[[Category: Bridger, W A.]] | [[Category: Bridger, W A.]] | ||
[[Category: Fraser, M E.]] | [[Category: Fraser, M E.]] | ||
[[Category: James, M N.G.]] | [[Category: James, M N.G.]] | ||
[[Category: Wolodko, W T.]] | [[Category: Wolodko, W T.]] | ||
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Revision as of 05:33, 3 May 2008
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 Page seeded by OCA on Sat May 3 08:33:20 2008
