1w8o

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[[Image:1w8o.gif|left|200px]]
[[Image:1w8o.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1w8o |SIZE=350|CAPTION= <scene name='initialview01'>1w8o</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1w8o", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1w8o| PDB=1w8o | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS'''
'''CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS'''
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[[Category: Watson, J N.]]
[[Category: Watson, J N.]]
[[Category: 3d-structure]]
[[Category: 3d-structure]]
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[[Category: beta-propeller]]
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[[Category: Beta-propeller]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: sialidase]]
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[[Category: Sialidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:18:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:32:45 2008''
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Revision as of 10:18, 3 May 2008

Template:STRUCTURE 1w8o

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 Sat May 3 13:18:41 2008

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