1mli
From Proteopedia
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CRYSTAL STRUCTURE OF MUCONOLACTONE ISOMERASE AT 3.3 ANGSTROMS RESOLUTION
Overview
The crystal structure of muconolactone isomerase from Pseudomonas putida, a unique molecule with ten 96 amino acid subunits and 5-fold, and 2-fold symmetries, has been solved at 3.3 A resolution. The non-crystallographic symmetries were used to refine the initial single isomorphous replacement phases and produce an interpretable 10-fold averaged map. The backbone trace is complete and confirmed by the amino acid sequence fit. Each subunit is composed of a body with two alpha-helices and an antiparallel twisted beta-sheet of four strands, and an extended arm. The helices and the sheet fold to form a two-layered structure with an enclosed hydrophobic core and a partially formed putative active site pocket. The C-terminal arm of another subunit related by a local dyad symmetry extends over the core to complete this pocket. The decameric protein is almost spherical, with the helices forming the external coat. There is a large hydrophilic cavity in the center with open ends along the 5-fold axis. Molecular interactions between subunits are extensive. Each subunit contacts four neighbors and loses nearly 40% of its solvent contact area on oligomerization.
About this Structure
1MLI is a Single protein structure of sequence from Pseudomonas putida. Active as Muconolactone Delta-isomerase, with EC number 5.3.3.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of muconolactone isomerase at 3.3 A resolution., Katti SK, Katz BA, Wyckoff HW, J Mol Biol. 1989 Feb 5;205(3):557-71. PMID:2926818
Page seeded by OCA on Thu Feb 21 13:56:24 2008
