2g7f
From Proteopedia
The 1.95 A crystal structure of Vibrio cholerae extracellular endonuclease I
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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