This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2pu3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pu3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pu3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pu3| PDB=2pu3 | SCENE= }}
{{STRUCTURE_2pu3| PDB=2pu3 | SCENE= }}
-
'''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===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18391403}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18391403 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18391403}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Salt adaptation]]
[[Category: Salt adaptation]]
[[Category: Structure]]
[[Category: Structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:33:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:26:46 2008''

Revision as of 04:26, 29 July 2008

Image:2pu3.png

Template:STRUCTURE 2pu3

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

Template:ABSTRACT PUBMED 18391403

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 Tue Jul 29 07:26:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pu3"
Personal tools