1gq9
From Proteopedia
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'''THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CTP AT 100K''' | '''THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CTP AT 100K''' | ||
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[[Category: Jelakovic, S.]] | [[Category: Jelakovic, S.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: | + | [[Category: Cmp-kdo synthetase]] |
| - | [[Category: | + | [[Category: Lipopolysaccharide biosynthesis]] |
| - | [[Category: | + | [[Category: Nucleoside monophosphate glycoside]] |
| - | [[Category: | + | [[Category: Nucleotidyltransferase]] |
| - | [[Category: | + | [[Category: Sugar-activating enzyme]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:53:10 2008'' | |
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Revision as of 14:53, 2 May 2008
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 CMP-Kdo was produced in a crystal and stabilized by freezing to 100 K. Its formation is accompanied by an induced fit involving mainchain displacements in the 2 A range. The observed binding conformations together with the amino acid conservation pattern during evolution and the putative location of the required Mg(2+) ion suggest a reaction pathway. The enzyme is structurally homologous to the CMP-N-acetylneuraminic acid synthetases in all parts except for the dimer interface. Moreover, the chainfold and the substrate-binding positions resemble those of other enzymes processing nucleotide sugars.
About this Structure
1GQ9 is a Single protein structure of sequence from Escherichia coli. 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 Page seeded by OCA on Fri May 2 17:53:10 2008
