1MLI

CRYSTAL STRUCTURE OF MUCONOLACTONE ISOMERASE AT 3.3 ANGSTROMS RESOLUTION

Summary for 1MLI

• Entry DOI: 10.2210/pdb1mli/pdb
• Descriptor: MUCONOLACTONE ISOMERASE (1 entity in total)
• Functional Keywords: intramolecular oxidoreductase
• Biological source: Pseudomonas putida
• Total number of polymer chains: 10
• Total formula weight: 111758.33

Authors

Katti, S.K.,Katz, B.A.,Wyckoff, H.W. (deposition date: 1989-11-02, release date: 1990-10-15, Last modification date: 2024-02-14)

Primary citation

Katti, S.K.,Katz, B.A.,Wyckoff, H.W.
Crystal structure of muconolactone isomerase at 3.3 A resolution.
J.Mol.Biol., 205:557-571, 1989

PubMed Abstract: 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.

PubMed: 2926818
DOI: 10.1016/0022-2836(89)90226-X

Experimental method

X-RAY DIFFRACTION (3.3 Å)