1w8o
From Proteopedia
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|PDB= 1w8o |SIZE=350|CAPTION= <scene name='initialview01'>1w8o</scene>, resolution 1.70Å | |PDB= 1w8o |SIZE=350|CAPTION= <scene name='initialview01'>1w8o</scene>, resolution 1.70Å | ||
|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LBT:LACTOSE'>LBT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w8o OCA], [http://www.ebi.ac.uk/pdbsum/1w8o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w8o RCSB]</span> | ||
}} | }} | ||
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[[Category: Taylor, G.]] | [[Category: Taylor, G.]] | ||
[[Category: Watson, J N.]] | [[Category: Watson, J N.]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: LBT]] | ||
| - | [[Category: NA]] | ||
[[Category: 3d-structure]] | [[Category: 3d-structure]] | ||
[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
| Line 38: | Line 37: | ||
[[Category: sialidase]] | [[Category: sialidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:32:45 2008'' |
Revision as of 21:32, 30 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Exo-alpha-sialidase, with EC number 3.2.1.18 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 00:32:45 2008
