1doc

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(New page: 200px<br /><applet load="1doc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1doc, resolution 2.0&Aring;" /> '''THE MOBIL FLAVIN OF 4...)
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Revision as of 11:19, 20 November 2007

Image:1doc.gif

1doc, resolution 2.0Å

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

Overview

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.

About this Structure

1DOC is a Single protein structure of sequence from Pseudomonas aeruginosa with BR, FAD and PHB as ligands. Full crystallographic information is available from OCA.

Reference

The mobile flavin of 4-OH benzoate hydroxylase., Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML, Science. 1994 Oct 7;266(5182):110-4. PMID:7939628

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