2pu3
From Proteopedia
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'''Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida''' | '''Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida''' | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
2PU3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_salmonicida_lfi1238 Vibrio salmonicida lfi1238]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PU3 OCA]. | 2PU3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_salmonicida_lfi1238 Vibrio salmonicida lfi1238]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PU3 OCA]. | ||
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| + | ==Reference== | ||
| + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18391403 18391403] | ||
[[Category: Deoxyribonuclease I]] | [[Category: Deoxyribonuclease I]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Salt adaptation]] | [[Category: Salt adaptation]] | ||
[[Category: Structure]] | [[Category: Structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:33:02 2008'' |
Revision as of 06:33, 28 May 2008
Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida
Overview
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.
About this Structure
2PU3 is a Single protein structure of sequence from Vibrio salmonicida lfi1238. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Wed May 28 09:33:02 2008
