1cs1
From Proteopedia
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[[Category: methionine biosynthesis]] | [[Category: methionine biosynthesis]] | ||
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Revision as of 12:55, 30 October 2007
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CYSTATHIONINE GAMMA-SYNTHASE (CGS) FROM ESCHERICHIA COLI
Overview
The transsulfuration enzyme cystathionine gamma-synthase (CGS) catalyses, the pyridoxal 5'-phosphate (PLP)-dependent gamma-replacement of, O-succinyl-L-homoserine and L-cysteine, yielding L-cystathionine. The, crystal structure of the Escherichia coli enzyme has been solved by, molecular replacement with the known structure of cystathionine beta-lyase, (CBL), and refined at 1.5 A resolution to a crystallographic R-factor of, 20.0%. The enzyme crystallizes as an alpha4 tetramer with the subunits, related by non-crystallographic 222 symmetry. The spatial fold of the, subunits, with three functionally distinct domains and their quaternary, arrangement, is similar to that of CBL. Previously proposed reaction, mechanisms for CGS can be checked against the structural model, allowing, ... [(full description)]
About this Structure
1CS1 is a [Single protein] structure of sequence from [Escherichia coli] with DHD as [ligand]. Active as [Transferred entry: 2.5.1.48], with EC number [4.2.99.9]. Structure known Active Sites: PLA, PLB, PLC and PLD. Full crystallographic information is available from [OCA].
Reference
Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution., Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A, EMBO J. 1998 Dec 1;17(23):6827-38. PMID:9843488
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