1RTT

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

Summary for 1RTT

• Entry DOI: 10.2210/pdb1rtt/pdb
• Descriptor: conserved hypothetical protein, SULFATE ION (3 entities in total)
• Functional Keywords: protein structure initiative, sad with sulfur, putative reductase, psi, new york sgx research center for structural genomics, nysgxrc, structural genomics, unknown function
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 21214.90

Authors

Agarwal, R.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-12-10, release date: 2004-08-17, Last modification date: 2024-02-14)

Primary citation

Agarwal, R.,Bonanno, J.B.,Burley, S.K.,Swaminathan, S.
Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.
ACTA CRYSTALLOGR.,SECT.D, 62:383-391, 2006

PubMed 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 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.

PubMed: 16552139
DOI: 10.1107/S0907444906001600

Experimental method

X-RAY DIFFRACTION (1.28 Å)