1DOE

THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS

Summary for 1DOE

• Entry DOI: 10.2210/pdb1doe/pdb
• Descriptor: P-HYDROXYBENZOATE HYDROXYLASE, BROMIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 45482.03

Authors

Gatti, D.L.,Palfey, B.A.,Lah, M.S.,Entsch, B.,Massey, V.,Ballou, D.P.,Ludwig, M.L. (deposition date: 1994-09-06, release date: 1994-11-30, Last modification date: 2024-02-07)

Primary citation

Gatti, D.L.,Palfey, B.A.,Lah, M.S.,Entsch, B.,Massey, V.,Ballou, D.P.,Ludwig, M.L.
The mobile flavin of 4-OH benzoate hydroxylase.
Science, 266:110-114, 1994

PubMed Abstract: Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis.

PubMed: 7939628

Experimental method

X-RAY DIFFRACTION (2.3 Å)