1rtt

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spinqualitylabelsall models 1rtt, resolution 1.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure determination of a putative NADH-dependent reductase using sulfur anomalous signal

Overview

The availability of high-intensity synchrotron facilities, technological, advances in data-collection techniques and improved data-reduction and, crystallographic software have ushered in a new era in high-throughput, macromolecular crystallography. Here, the de novo automated crystal, structure determination at 1.28 A resolution of an NAD(P)H-dependent FMN, reductase flavoprotein from Pseudomonas aeruginosa PA01-derived protein, Q9I4D4 using the anomalous signal from an unusually small number of S, atoms is reported. Although this protein lacks the flavodoxin key, fingerprint motif [(T/S)XTGXT], it has been confirmed to bind flavin, mononucleotide and the binding site was identified via X-ray, crystallography. This protein contains a novel flavin, mononucleotide-binding site GSLRSGSYN, which has not been previously, reported. Detailed statistics pertaining to sulfur phasing and other, factors contributing to structure determination are discussed. Structural, comparisons of the apoenzyme and the protein complexed with flavin, mononucleotide show conformational changes on cofactor binding., NADPH-dependent activity has been confirmed with biochemical assays.

About this Structure

1RTT is a Single protein structure of sequence from Pseudomonas aeruginosa pao1 with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal., Agarwal R, Bonanno JB, Burley SK, Swaminathan S, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):383-91. Epub 2006, Mar 18. PMID:16552139

Page seeded by OCA on Sat Nov 24 23:14:35 2007