1JOF

Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme

Summary for 1JOF

• Entry DOI: 10.2210/pdb1jof/pdb
• Related: 1MUC
• Descriptor: CARBOXY-CIS,CIS-MUCONATE CYCLASE, SULFATE ION, BETA-MERCAPTOETHANOL, ... (5 entities in total)
• Functional Keywords: beta-propeller, homotetramer, semet-protein, isomerase
• Biological source: Neurospora crassa
• Total number of polymer chains: 8
• Total formula weight: 336346.68

Authors

Kajander, T.,Merckel, M.C.,Thompson, A.,Deacon, A.M.,Mazur, P.,Kozarich, J.W.,Goldman, A. (deposition date: 2001-07-28, release date: 2002-04-12, Last modification date: 2021-10-27)

Primary citation

Kajander, T.,Merckel, M.C.,Thompson, A.,Deacon, A.M.,Mazur, P.,Kozarich, J.W.,Goldman, A.
The structure of Neurospora crassa 3-carboxy-cis,cis-muconate lactonizing enzyme, a beta propeller cycloisomerase.
Structure, 10:483-492, 2002

PubMed Abstract: 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.

PubMed: 11937053
DOI: 10.1016/S0969-2126(02)00744-X

Experimental method

X-RAY DIFFRACTION (2.5 Å)