2g7e
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(New page: 200px<br /><applet load="2g7e" size="350" color="white" frame="true" align="right" spinBox="true" caption="2g7e, resolution 1.600Å" /> '''The 1.6 A crystal s...)
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Revision as of 17:53, 29 January 2008
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The 1.6 A crystal structure of Vibrio cholerae extracellular endonuclease I
Overview
The crystal structure of a periplasmic/extracellular endonuclease from, Vibrio cholerae has been solved at low and at neutral pH. Crystals grown, at pH 4.6 and 6.9 diffracted to 1.6 A (on BM01A at the ESRF) and 1.95 A, (on a rotating-anode generator), respectively. The structures of the, endonuclease were compared with the structure of a homologous enzyme in V., vulnificus. The structures of the V. cholerae enzyme at different pH, values are essentially identical to each other and to the V. vulnificus, enzyme. However, interesting features were observed in the solvent, structures. Both V. cholerae structures reveal the presence of a chloride, ion completely buried within the core of the protein, with the nearest, solvent molecule approximately 7 A away. Magnesium, which is essential for, catalysis, is present in the structure at neutral pH, but is absent at low, pH, and may partly explain the inactivity of the enzyme at lower pH.
About this Structure
2G7E is a Single protein structure of sequence from Vibrio cholerae with as ligand. Active as Deoxyribonuclease I, with EC number 3.1.21.1 Full crystallographic information is available from OCA.
Reference
The structure of Vibrio cholerae extracellular endonuclease I reveals the presence of a buried chloride ion., Altermark B, Smalas AO, Willassen NP, Helland R, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1387-91. Epub 2006, Oct 18. PMID:17057343
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