Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase.
The New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex.
Kniewel
Ryan
R
Biochemistry Department and Structural Biology Program, Weill Medical College of Cornell University, New York, NY 10021, USA.
Buglino
John A
JA
Shen
Vincent
V
Chadha
Tanya
T
Beckwith
Andrew
A
Lima
Christopher D
CD
D001665:Binding Sites; D018360:Crystallography, X-Ray; D007295:Inositol Phosphates / Q000096:biosynthesis; D008958:Models, Molecular; D007296:Myo-Inositol-1-Phosphate Synthase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D009243:NAD / Q000737:chemistry; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013329:Structure-Activity Relationship
D007295:Inositol Phosphates; D029701:Saccharomyces cerevisiae Proteins; D009243:NAD; C002647:inositol 1-phosphate; D007296:Myo-Inositol-1-Phosphate Synthase