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| {{STRUCTURE_1jof| PDB=1jof | SCENE= }} | | {{STRUCTURE_1jof| PDB=1jof | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11937053}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11937053 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11937053}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Homotetramer]] | | [[Category: Homotetramer]] |
| [[Category: Semet-protein]] | | [[Category: Semet-protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:30:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:33:16 2008'' |
