1w8o

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[[Image:1w8o.gif|left|200px]]<br /><applet load="1w8o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w8o.gif|left|200px]]
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caption="1w8o, resolution 1.70&Aring;" />
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'''CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS'''<br />
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{{Structure
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|PDB= 1w8o |SIZE=350|CAPTION= <scene name='initialview01'>1w8o</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=LBT:LACTOSE'>LBT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1W8O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Micromonospora_viridifaciens Micromonospora viridifaciens] with <scene name='pdbligand=LBT:'>LBT</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W8O OCA].
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1W8O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Micromonospora_viridifaciens Micromonospora viridifaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W8O OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15527797 15527797]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15527797 15527797]
[[Category: Exo-alpha-sialidase]]
[[Category: Exo-alpha-sialidase]]
[[Category: Micromonospora viridifaciens]]
[[Category: Micromonospora viridifaciens]]
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[[Category: sialidase]]
[[Category: sialidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:41 2008''

Revision as of 12:53, 20 March 2008

Image:1w8o.gif


PDB ID 1w8o

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites:
Ligands: , , and
Activity: Exo-alpha-sialidase, with EC number 3.2.1.18
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 Thu Mar 20 14:53:41 2008

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