2pu3 | pdb_00002pu3

Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida

spinqualitylabelsall models 2pu3, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pu3 is a 1 chain structure with sequence from Aliivibrio salmonicida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MG Related: 2g7e, 2g7f Activity: Deoxyribonuclease I, with EC number 3.1.21.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of the periplasmic/extracellular endonuclease I from Vibrio salmonicida has been solved to 1.5 A resolution and, in comparison to the corresponding endonucleases from V. cholerae and V. vulnificus, serves as a model system for the investigation of the structural determinants involved in the temperature and NaCl adaptation of this enzyme class. The overall fold of the three enzymes is essentially similar, but the V. salmonicida endonuclease displays a significantly more positive surface potential than the other two enzymes owing to the presence of ten more Lys residues. However, if the optimum salt concentrations for the V. salmonicida and V. cholerae enzymes are taken into consideration in the electrostatic surface-potential calculation, the potentials of the two enzymes become surprisingly similar. The higher number of basic residues in the V. salmonicida protein is therefore likely to be a result, at least in part, of adaptation to the more saline habitat of V. salmonicida (seawater) than V. cholerae (brackish water). The hydrophobic core of all three enzymes is almost identical, but the V. salmonicida endonuclease has a slightly lower number of internal hydrogen bonds. This, together with repulsive forces between the basic residues on the protein surface of V. salmonicida endonuclease I and differences in the distribution of salt bridges, probably results in higher flexibility of regions of the V. salmonicida protein. This is likely to influence both the catalytic activity and the stability of the protein. Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida.,Altermark B, Helland R, Moe E, Willassen NP, Smalas AO Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):368-76. Epub 2008, Mar 19. PMID:18391403 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease

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