1w8o
From Proteopedia
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| - | [[Image:1w8o.gif|left|200px]]<br /> | + | [[Image:1w8o.gif|left|200px]]<br /><applet load="1w8o" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1w8o" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1w8o, resolution 1.70Å" /> | caption="1w8o, resolution 1.70Å" /> | ||
'''CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS'''<br /> | '''CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 LBT, NA, CIT and GOL 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] | + | 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 LBT, NA, CIT and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W8O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sialidase]] | [[Category: sialidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:34:40 2007'' |
Revision as of 16:24, 18 December 2007
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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 with LBT, NA, CIT and GOL as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Known structural/functional Site: . 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 Tue Dec 18 18:34:40 2007
Categories: Exo-alpha-sialidase | Micromonospora viridifaciens | Single protein | Bennet, A.J. | Dookhun, V. | Newstead, S. | Taylor, G. | Watson, J.N. | CIT | GOL | LBT | NA | 3d-structure | Beta-propeller | Glycosidase | Hydrolase | Sialidase
