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1h7g
From Proteopedia
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Revision as of 13:26, 30 October 2007
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THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE AND OF ITS COMPLEXES WITH SUBSTRATES AND SUBSTRATE ANALOGUES, CTP MG2+ COMPLEX
Overview
The enzyme CMP-Kdo synthetase (CKS) catalyzes the activation of the sugar, Kdo (2-keto-3-deoxy-manno-octonic acid) by forming a monophosphate, diester. CKS is a pharmaceutical target because CMP-Kdo is used in the, biosynthesis of lipopolysaccharides that are vital for Gram-negative, bacteria. We have refined the structure of the unligated capsule-specific, CKS from Escherichia coli at 1.8 A resolution (1 A=0.1 nm) and we have, established the structures of its complexes with the substrate CTP, with, CDP and CMP as well as with the product analog CMP-NeuAc (CMP-sialate) by, X-ray diffraction analyses at resolutions between 2.1 A and 2.5 A. The, N-terminal domains of the dimeric enzyme bind CTP in a peculiar, nucleotide-binding fold, whereas the C-terminal domains form the dimer, ... [(full description)]
About this Structure
1H7G is a [Single protein] structure of sequence from [Escherichia coli] with MG and CTP as [ligands]. Active as [3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [2.7.7.38]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [OCA].
Reference
The structure of CMP:2-keto-3-deoxy-manno-octonic acid synthetase and of its complexes with substrates and substrate analogs., Jelakovic S, Schulz GE, J Mol Biol. 2001 Sep 7;312(1):143-55. PMID:11545592
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