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1w8n

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1w8n, resolution 2.10Å ()
Ligands: , ,
Activity: Exo-alpha-sialidase, with EC number 3.2.1.18
Related: 1eur, 1eus, 1eut, 1euu
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

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

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1w8n is a 1 chain structure with sequence from Micromonospora viridifaciens. Full crystallographic information is available from OCA.

See Also

Reference

  • Watson JN, Newstead S, Dookhun V, Taylor G, Bennet AJ. Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens. FEBS Lett. 2004 Nov 5;577(1-2):265-9. PMID:15527797 doi:10.1016/j.febslet.2004.10.016

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