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1gq9
From Proteopedia
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Revision as of 13:12, 30 October 2007
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THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CTP AT 100K
Overview
The activation of the sugar 2-keto-3-deoxy-manno-octonic acid (Kdo) is, catalyzed by CMP-Kdo synthetase (EC 2.7.7.38) and results in a, monophosphate diester with CMP. The enzyme is a pharmaceutical target, because CMP-Kdo is required for the biosynthesis of lipopolysaccharides, that are vital for Gram-negative bacteria. We have established the, structures of an enzyme complex with the educt CTP and of a complex with, the product CMP-Kdo by X-ray diffraction analyses at 100 K, both at 2.6 A, resolution. The N-terminal domains of the dimeric enzyme bind CTP in a, peculiar nucleotide-binding fold with the beta- and gamma-phosphates, located at the so-called "PP-loop", whereas the C-terminal domains, participate in Kdo binding and in the dimer interface. The unstable, nucleotide-sugar ... [(full description)]
About this Structure
1GQ9 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 Site: CTA. Full crystallographic information is available from [OCA].
Reference
Catalytic mechanism of CMP:2-keto-3-deoxy-manno-octonic acid synthetase as derived from complexes with reaction educt and product., Jelakovic S, Schulz GE, Biochemistry. 2002 Jan 29;41(4):1174-81. PMID:11802716
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