1w8o

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spinqualitylabelsall models 1w8o, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS

Overview

A recombinant D92G mutant sialidase from Micromonospora viridifaciens has, been cloned, expressed and purified. Kinetic studies reveal that the, replacement of the conserved aspartic acid with glycine results in a, catalytically competent retaining sialidase that possesses significant, activity against activated substrates. The contribution of this aspartate, residue to the free energy of hydrolysis for natural substrates is greater, than 19 kJ/mol. The three dimensional structure of the D92G mutant shows, that the removal of aspartic acid 92 causes no significant re-arrangement, of the active site, and that an ordered water molecule substitutes for the, carboxylate group of D92.

About this Structure

1W8O is a [Single protein] structure of sequence from [Micromonospora viridifaciens] with LBT, NA, CIT and GOL as [ligands]. Active as [[1]], with EC number [3.2.1.18]. Full crystallographic information is available from [OCA].

Reference

Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens., Watson JN, Newstead S, Dookhun V, Taylor G, Bennet AJ, FEBS Lett. 2004 Nov 5;577(1-2):265-9. PMID:15527797

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