2dg0: Difference between revisions

Revision as of 16:08, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2dg0.png

Template:STRUCTURE 2dg0

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

Template:ABSTRACT PUBMED 17166853

About this StructureAbout this Structure

2DG0 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus'''
+===Crystal structure 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
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 ==About this Structure==
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 [[Category: Yao, M.]]
 [[Category: Beta propeller]]
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