1muc
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1muc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1muc, resolution 1.85Å" /> '''STRUCTURE OF MUCONA...)
Next diff →
Revision as of 16:01, 29 October 2007
|
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 [[1]], with EC number [5.5.1.1]. 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
Page seeded by OCA on Mon Oct 29 18:06:30 2007
