1jof
From Proteopedia
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'''Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme''' | '''Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme''' | ||
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[[Category: Merckel, M C.]] | [[Category: Merckel, M C.]] | ||
[[Category: Thompson, A.]] | [[Category: Thompson, A.]] | ||
- | [[Category: | + | [[Category: Beta-propeller]] |
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Revision as of 18:30, 2 May 2008
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 Fri May 2 21:30:12 2008