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.


2dso

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2dso.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2dso.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2dso| PDB=2dso | SCENE= }}
{{STRUCTURE_2dso| PDB=2dso | SCENE= }}
-
'''Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus'''
+
===Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus===
-
==Overview==
+
<!--
-
Drp35 is a protein induced by cell wall-affecting antibiotics or detergents; it possesses calcium-dependent lactonase activity. To determine the molecular basis of the lactonase activity, we first solved the crystal structures of Drp35 with and without Ca(2+); these showed that the molecule has a six-bladed beta-propeller structure with two calcium ions bound at the center of the beta-propeller and surface region. Mutational analyses of evolutionarily conserved residues revealed that the central calcium-binding site is essential for the enzymatic activity of Drp35. Substitution of some other amino acid residues for the calcium-binding residues demonstrated the critical contributions of Glu(48), Asp(138), and Asp(236) to the enzymatic activity. Differential scanning calorimetric analysis revealed that the loss of activity of E48Q and D236N, but not D138N, was attributed to their inability to hold the calcium ion. Further structural analysis of the D138N mutant indicates that it lacks a water molecule bound to the calcium ion rather than the calcium ion itself. Based on these observations and structural information, a possible catalytic mechanism in which the calcium ion and its binding residues play direct roles was proposed for the lactonase activity of Drp35.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17166853}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17166853 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17166853}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Yao, M.]]
[[Category: Yao, M.]]
[[Category: Beta propeller]]
[[Category: Beta propeller]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:10:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:06:19 2008''

Revision as of 12:06, 29 July 2008

Image:2dso.png

Template:STRUCTURE 2dso

Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus

Template:ABSTRACT PUBMED 17166853

About this Structure

2DSO is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity., Tanaka Y, Morikawa K, Ohki Y, Yao M, Tsumoto K, Watanabe N, Ohta T, Tanaka I, J Biol Chem. 2007 Feb 23;282(8):5770-80. Epub 2006 Dec 13. PMID:17166853

Page seeded by OCA on Tue Jul 29 15:06:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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