1eyr
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(New page: 200px<br /><applet load="1eyr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eyr, resolution 2.20Å" /> '''Structure of a siali...)
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Revision as of 12:19, 20 November 2007
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Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP
Overview
The x-ray crystallographic structure of selenomethionyl, cytosine-5'-monophosphate-acylneuraminate synthetase (CMP-NeuAc, synthetase) from Neisseria meningitidis has been determined at 2.0-A, resolution using multiple-wavelength anomalous dispersion phasing, and a, second structure, in the presence of the substrate analogue CDP, has been, determined at 2.2-A resolution by molecular replacement. This work, identifies the active site residues for this class of enzyme for the first, time. The detailed interactions between the enzyme and CDP within the, mononucleotide-binding pocket are directly observed, and the, acylneuraminate-binding pocket has also been identified. A model of, acylneuraminate bound to CMP-NeuAc synthetase has been constructed and, provides a structural basis for understanding the mechanism of production, of "activated" sialic acids. Sialic acids are key saccharide components on, the surface of mammalian cells and can be virulence factors in a variety, of bacterial species (e.g. Neisseria, Haemophilus, group B streptococci, etc.). As such, the identification of the bacterial CMP-NeuAc synthetase, active site can serve as a starting point for rational drug design, strategies.
About this Structure
1EYR is a Single protein structure of sequence from Neisseria meningitidis with CDP as ligand. Active as N-acylneuraminate cytidylyltransferase, with EC number 2.7.7.43 Full crystallographic information is available from OCA.
Reference
Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP., Mosimann SC, Gilbert M, Dombroswki D, To R, Wakarchuk W, Strynadka NC, J Biol Chem. 2001 Mar 16;276(11):8190-6. Epub 2000 Dec 11. PMID:11113120
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