1qjv: Difference between revisions
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Revision as of 13:56, 30 October 2007
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PECTIN METHYLESTERASE PEMA FROM ERWINIA CHRYSANTHEMI
Overview
Most structures of neutral lipases and esterases have been found to adopt, the common alpha/beta hydrolase fold and contain a catalytic Ser-His-Asp, triad. Some variation occurs in both the overall protein fold and in the, location of the catalytic triad, and in some enzymes the role of the, aspartate residue is replaced by a main-chain carbonyl oxygen atom. Here, we report the crystal structure of pectin methylesterase that has neither, the common alpha/beta hydrolase fold nor the common catalytic triad. The, structure of the Erwinia chrysanthemi enzyme was solved by multiple, isomorphous replacement and refined at 2.4 A to a conventional, crystallographic R-factor of 17.9 % (R(free) 21.1 %). This is the first, structure of a pectin methylesterase and reveals the enzyme to comprise a, ... [(full description)]
About this Structure
1QJV is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with CL as [ligand]. Active as [Pectinesterase], with EC number [3.1.1.11]. Structure known Active Sites: PMA and PMB. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site., Jenkins J, Mayans O, Smith D, Worboys K, Pickersgill RW, J Mol Biol. 2001 Jan 26;305(4):951-60. PMID:11162105
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