1jof
From Proteopedia
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| , resolution 2.5Å | |||||||
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| Ligands: | , , , | ||||||
| Activity: | Carboxy-cis,cis-muconate cyclase, with EC number 5.5.1.5 | ||||||
| Related: | 1MUC
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 21:36:33 2008
