2WSI

Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD

Summary for 2WSI

• Entry DOI: 10.2210/pdb2wsi/pdb
• Descriptor: FAD SYNTHETASE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: transferase, nucleotidyltransferase, nucleotide-binding
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Cytoplasm: P38913
• Total number of polymer chains: 1
• Total formula weight: 36462.64

Authors

Leulliot, N.,van Tilbeurgh, H. (deposition date: 2009-09-07, release date: 2010-05-26, Last modification date: 2024-05-08)

Primary citation

Leulliot, N.,Blondeau, K.,Keller, J.,Ulryck, N.,Quevillon-Cheruel, S.,Van Tilbeurgh, H.
Crystal Structure of Yeast Fad Synthetase (Fad1) in Complex with Fad.
J.Mol.Biol., 398:641-, 2010

PubMed Abstract: Flavin adenine dinucleotide (FAD) synthetase is an essential enzyme responsible for the synthesis of FAD by adenylation of riboflavin monophosphate (FMN). We have solved the 1.9 A resolution structure of Fad1, the yeast FAD synthetase, in complex with the FAD product in the active site. The structure of Fad1 shows it to be a member of the PP-ATPase superfamily. Important conformational differences in the two motifs involved in binding the phosphate moieties of FAD compared to the Candida glabrata FMNT ortholog suggests that this loop is dynamic and undergoes substantial conformational changes during its catalytic cycle.

PubMed: 20359485
DOI: 10.1016/J.JMB.2010.03.040

Experimental method

X-RAY DIFFRACTION (1.9 Å)