1jof
From Proteopedia
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Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme
Overview
Muconate lactonizing enzymes (MLEs) convert cis,cis-muconates to, muconolactones in microbes as part of the beta-ketoadipate pathway; some, also dehalogenate muconate derivatives of xenobiotic haloaromatics. There, are three different MLE classes unrelated by evolution. We present the, X-ray structure of a eukaryotic MLE, Neurospora crassa, 3-carboxy-cis,cis-muconate lactonizing enzyme (NcCMLE) at 2.5 A, resolution, with a seven-bladed beta propeller fold. It is related neither, to bacterial MLEs nor to other beta propeller enzymes, but is structurally, similar to the G protein beta subunit. It reveals a novel, metal-independent cycloisomerase motif unlike the bacterial metal cofactor, MLEs. Together, the bacterial MLEs and NcCMLE structures comprise a, striking structural example of functional convergence in enzymes for, 1,2-addition-elimination of carboxylic acids. NcCMLE and bacterial MLEs, may enhance the reaction rate differently: the former by electrophilic, catalysis and the latter by electrostatic stabilization of the enolate.
About this Structure
1JOF is a Single protein structure of sequence from Neurospora crassa with SO4, PIN and BME as ligands. Active as Carboxy-cis,cis-muconate cyclase, with EC number 5.5.1.5 Full crystallographic information is available from OCA.
Reference
The structure of Neurospora crassa 3-carboxy-cis,cis-muconate lactonizing enzyme, a beta propeller cycloisomerase., Kajander T, Merckel MC, Thompson A, Deacon AM, Mazur P, Kozarich JW, Goldman A, Structure. 2002 Apr;10(4):483-92. PMID:11937053
Page seeded by OCA on Tue Nov 20 18:25:25 2007
