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1muc
From Proteopedia
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[[Category: muconate lactonizing enzyme]] | [[Category: muconate lactonizing enzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:43:23 2007'' |
Revision as of 13:38, 30 October 2007
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STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION
Overview
We report here the refined X-ray crystal structure of muconate lactonizing, enzyme (MLE) from Pseudomonas putida PRS2000 at a resolution of 1.85 A, with an R-factor of 16.8%. An enzyme from the beta-ketoadipate pathway, MLE catalyses the conversion of cis,cis-muconate to muconolactone. It is a, homo-octamer, one monomer consisting of 373 amino acid residues. MLE has, two large domains and a C-terminal subdomain: an alpha + beta domain, an, alpha beta-barrel domain and a C-terminal meandering subdomain. The alpha, beta-barrel domain is highly irregular. Its structure is (beta/alpha)7, beta, with the structural role of the last alpha-helix being replaced by, both the C-terminal subdomain and part of the N-terminal domain. The, fifth, seventh and eighth barrel strands are unusual because ... [(full description)]
About this Structure
1MUC is a [Single protein] structure of sequence from [Pseudomonas putida] with MN as [ligand]. This structure superseeds the now removed PDB entry 1MLE. Active as [Muconate cycloisomerase], with EC number [5.5.1.1]. Structure known Active Sites: MNA and MNB. Full crystallographic information is available from [OCA].
Reference
The refined X-ray structure of muconate lactonizing enzyme from Pseudomonas putida PRS2000 at 1.85 A resolution., Helin S, Kahn PC, Guha BL, Mallows DG, Goldman A, J Mol Biol. 1995 Dec 15;254(5):918-41. PMID:7500361
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