1nsd

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[[Image:1nsd.gif|left|200px]]
[[Image:1nsd.gif|left|200px]]
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{{Structure
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|PDB= 1nsd |SIZE=350|CAPTION= <scene name='initialview01'>1nsd</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1nsd", creates the "Structure Box" on the page.
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|SITE=
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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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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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|DOMAIN=
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{{STRUCTURE_1nsd| PDB=1nsd | 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=1nsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsd OCA], [http://www.ebi.ac.uk/pdbsum/1nsd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nsd RCSB]</span>
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}}
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'''INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR'''
'''INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR'''
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[[Category: Cusack, S.]]
[[Category: Cusack, S.]]
[[Category: Ruigrok, R W.H.]]
[[Category: Ruigrok, R W.H.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:55:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:34:51 2008''
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Revision as of 23:55, 2 May 2008

Image:1nsd.gif

Template:STRUCTURE 1nsd

INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR


Overview

BACKGROUND: Neuraminidase, one of the two surface glycoproteins of influenza virus, cleaves terminal sialic acid residues from glycolipids or glycoproteins. Its crystal structure is known at high resolution, but the mechanism of glycosyl hydrolysis remains unclear. RESULTS: We have determined the crystal structure at 1.8 A resolution of two complexes of influenza B/Beijing neuraminidase containing either the reaction product, sialic acid, or the transition state analogue inhibitor, 2,3-dehydro-2-deoxy-N-acetylneuraminic acid (DANA). The sialic acid is bound in a distorted 'boat' conformation closely resembling that of bound DANA, stabilized by a conserved tyrosine residue (Tyr408). This distortion also gives rise to a suicidal side reaction that converts sialic acid to DANA at a low rate. CONCLUSIONS: The mechanism of neuraminidase action is distinct from that of other known glycosyl hydrolases. Substrate distortion appears to be the driving force in glycosyl bond hydrolysis and the proton required for catalysis can probably be donated by water, rather than by residues in the active site, thus allowing the enzyme to operate at high pH. The side reaction converting sialic acid to DANA appears reasonably favourable, and it is unclear how this is minimized by the enzyme.

About this Structure

1NSD is a Single protein structure of sequence from Influenza b virus. Full crystallographic information is available from OCA.

Reference

Influenza B virus neuraminidase can synthesize its own inhibitor., Burmeister WP, Henrissat B, Bosso C, Cusack S, Ruigrok RW, Structure. 1993 Sep 15;1(1):19-26. PMID:8069621 Page seeded by OCA on Sat May 3 02:55:15 2008

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