2vbs
From Proteopedia
|
RIBOFLAVIN KINASE MJ0056 FROM METHANOCALDOCOCCUS JANNASCHII IN COMPLEX WITH PO4
Overview
Proteins of the cradle-loop barrel metafold are formed by duplication of a, conserved betaalphabeta-element, suggesting a common evolutionary origin, from an ancestral group of nucleic acid-binding proteins. The basal fold, within this metafold, the RIFT barrel, is also found in a wide range of, enzymes, whose homologous relationship with the nucleic acid-binding group, is unclear. We have characterized a protein family that is intermediate in, sequence and structure between the basal group of cradle-loop barrels and, one family of RIFT-barrel enzymes, the riboflavin kinases. We report the, structure, substrate-binding mode, and catalytic activity for one of these, proteins, Methanocaldococcus jannaschii Mj0056, which is an archaeal, riboflavin kinase. Mj0056 is unusual in utilizing CTP rather than ATP as, the donor nucleotide, and sequence conservation in the relevant residues, suggests that this is a general feature of archaeal riboflavin kinases.
About this Structure
2VBS is a Single protein structure of sequence from Methanocaldococcus jannaschii with , and as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
A CTP-Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle-Loop Barrels., Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M, Structure. 2007 Dec;15(12):1577-90. PMID:18073108
Page seeded by OCA on Wed Jan 23 11:24:38 2008
