1rkd
From Proteopedia
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E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP
Overview
BACKGROUND: D-ribose must be phosphorylated at O5' before it can be used, in either anabolism or catabolism. This reaction is catalysed by, ribokinase and requires the presence of ATP and magnesium. Ribokinase is a, member of a family of carbohydrate kinases of previously unknown, structure. RESULTS: The crystal structure of ribokinase from Escherichia, coli in complex with ribose and dinucleotide was determined at 1.84 A, resolution by multiple isomorphous replacement. There is one 33 kDa, monomer of ribokinase in the asymmetric unit but the protein forms a dimer, around a crystallographic twofold axis. Each subunit consists of a central, alpha/beta unit, with a new type of nucleotide-binding fold, and a, distinct beta sheet that forms a lid over the ribose-binding site. Contact, between ... [(full description)]
About this Structure
1RKD is a [Single protein] structure of sequence from [Escherichia coli] with RIB, PO4 and ADP as [ligands]. Active as [Ribokinase], with EC number [2.7.1.15]. Structure known Active Sites: AB1, AB2, AB3, RB1, RB2 and RB3. Full crystallographic information is available from [OCA].
Reference
Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures., Sigrell JA, Cameron AD, Jones TA, Mowbray SL, Structure. 1998 Feb 15;6(2):183-93. PMID:9519409
Page seeded by OCA on Tue Oct 30 16:03:28 2007
Categories: Escherichia coli | Ribokinase | Single protein | Cameron, A.D. | Jones, T.A. | Mowbray, S.L. | Sigrell, J.A. | ADP | PO4 | RIB | Carbohydrate kinase | Nucleotide binding | Ribose | Transferase
