Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.

ABSTRACT: 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

SUBMITTER: Agarwal R 

PROVIDER: S-EPMC1431508 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature