1W8N
Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens.
Summary for 1W8N
| Entry DOI | 10.2210/pdb1w8n/pdb |
| Related | 1EUR 1EUS 1EUT 1EUU |
| Descriptor | BACTERIAL SIALIDASE, beta-D-galactopyranose, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID, ... (5 entities in total) |
| Functional Keywords | glycosidase, hydrolase, neuraminidase, beta- propeller fold. |
| Biological source | MICROMONOSPORA VIRIDIFACIENS |
| Cellular location | Secreted: Q02834 |
| Total number of polymer chains | 1 |
| Total formula weight | 64735.00 |
| Authors | Newstead, S.,Watson, J.N.,Dookhun, V.,Bennet, A.J.,Taylor, G. (deposition date: 2004-09-24, release date: 2004-09-30, Last modification date: 2024-11-06) |
| Primary citation | Watson, J.N.,Newstead, S.,Dookhun, V.,Taylor, G.,Bennet, A.J. Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora Viridifaciens FEBS Lett., 577:265-, 2004 Cited by PubMed Abstract: 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. PubMed: 15527797DOI: 10.1016/J.FEBSLET.2004.10.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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