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[[Image:1scu.gif|left|200px]]
{{Seed}}
[[Image:1scu.png|left|200px]]


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{{STRUCTURE_1scu|  PDB=1scu  |  SCENE=  }}  
{{STRUCTURE_1scu|  PDB=1scu  |  SCENE=  }}  


'''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===




==Overview==
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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.
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{{ABSTRACT_PUBMED_8144675}}


==About this Structure==
==About this Structure==
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[[Category: James, M N.G.]]
[[Category: James, M N.G.]]
[[Category: Wolodko, W T.]]
[[Category: Wolodko, W T.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:33:20 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:05:05 2008''

Revision as of 18:05, 28 July 2008

File:1scu.png

Template:STRUCTURE 1scu

THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8144675

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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