2jcd

From Proteopedia

Revision as of 20:59, 29 October 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

2jcd, resolution 2.11Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE N-OXYGENASE AURF FROM STREPTOMYCES THIOLUTEUS

Overview

Nitro groups are found in a number of bioactive compounds. Most of them, arise by a stepwise mono-oxygenation of amino groups. One of the involved, enzymes is AurF participating in the biosynthesis of aureothin. Its, structure was established at 2.1 A resolution showing a homodimer with a, binuclear manganese cluster. The enzyme preparation, which yielded the, analyzed crystals, showed activity using in vitro and in vivo assays., Chain fold and cluster are homologous with ribonucleotide reductase, subunit R2 and related enzymes. The two manganese ions and an iron content, of about 15% were established by anomalous X-ray diffraction. A comparison, of the cluster with more common di-iron clusters suggested an additional, histidine in the coordination sphere to cause the preference for ... [(full description)]

About this Structure

2JCD is a [Single protein] structure of sequence from [Streptomyces thioluteus] with MN and EDO as [ligands]. Full crystallographic information is available from [OCA].

Reference

Structure and Action of the N-oxygenase AurF from Streptomyces thioluteus., Zocher G, Winkler R, Hertweck C, Schulz GE, J Mol Biol. 2007 Jun 9;. PMID:17765264

Page seeded by OCA on Mon Oct 29 23:03:49 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools