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| - | [[Image:1scu.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1scu| PDB=1scu | SCENE= }} | | {{STRUCTURE_1scu| PDB=1scu | SCENE= }} |
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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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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8144675}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8144675 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8144675}} |
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| | ==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
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
Page seeded by OCA on Mon Jul 28 21:05:05 2008
