1nb9
From Proteopedia
|
Crystal Structure of Riboflavin Kinase
Overview
Riboflavin kinase (RFK) is an essential enzyme catalyzing the, phosphorylation of riboflavin (vitamin B(2)) to form FMN, an obligatory, step in vitamin B(2) utilization and flavin cofactor synthesis. The, structure of human RFK revealed a six-stranded antiparallel beta barrel, core structurally similar to the riboflavin synthase/ferredoxin reductase, FAD binding domain fold. The binding site of an intrinsically bound MgADP, defines a novel nucleotide binding motif that encompasses a loop, a 3(10), helix, and a reverse turn followed by a short beta strand. This active, site loop forms an arch with ATP and riboflavin binding at the opposite, side and the phosphoryl transfer appears to occur through the hole, underneath the arch. The invariant residues Asn36 and Glu86 are implicated, in the catalysis.
About this Structure
1NB9 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Riboflavin kinase, with EC number 2.7.1.26 Full crystallographic information is available from OCA.
Reference
Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch., Karthikeyan S, Zhou Q, Mseeh F, Grishin NV, Osterman AL, Zhang H, Structure. 2003 Mar;11(3):265-73. PMID:12623014
Page seeded by OCA on Fri Feb 15 16:28:01 2008
Categories: Homo sapiens | Riboflavin kinase | Single protein | Grishin, N.V. | Karthikeyan, S. | Mseeh, F. | Osterman, A.L. | Zhang, H. | Zhou, Q. | ADP | MG | RBF | Beta barrel | Riboflavin | Transferase
