1orr

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[[Image:1orr.jpg|left|200px]]
[[Image:1orr.jpg|left|200px]]
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{{Structure
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|PDB= 1orr |SIZE=350|CAPTION= <scene name='initialview01'>1orr</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1orr", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CDP:CYTIDINE-5&#39;-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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|GENE= RFBE OR STY2298 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=601 Salmonella typhi])
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|DOMAIN=
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{{STRUCTURE_1orr| PDB=1orr | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1orr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1orr OCA], [http://www.ebi.ac.uk/pdbsum/1orr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1orr RCSB]</span>
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'''Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP'''
'''Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP'''
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[[Category: Koropatkin, N M.]]
[[Category: Koropatkin, N M.]]
[[Category: Liu, H.]]
[[Category: Liu, H.]]
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[[Category: rossmann fold]]
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[[Category: Rossmann fold]]
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[[Category: short-chain dehydrogenase/reductase]]
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[[Category: Short-chain dehydrogenase/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:12:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:49:24 2008''
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Revision as of 01:12, 3 May 2008

Template:STRUCTURE 1orr

Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP


Overview

Tyvelose epimerase catalyzes the last step in the biosynthesis of tyvelose by converting CDP-d-paratose to CDP-d-tyvelose. This unusual 3,6-dideoxyhexose occurs in the O-antigens of some types of Gram-negative bacteria. Here we describe the cloning, protein purification, and high-resolution x-ray crystallographic analysis of tyvelose epimerase from Salmonella typhi complexed with CDP. The enzyme from S. typhi is a homotetramer with each subunit containing 339 amino acid residues and a tightly bound NAD+ cofactor. The quaternary structure of the enzyme displays 222 symmetry and can be aptly described as a dimer of dimers. Each subunit folds into two distinct lobes: the N-terminal motif responsible for NAD+ binding and the C-terminal region that harbors the binding site for CDP. The analysis described here demonstrates that tyvelose epimerase belongs to the short-chain dehydrogenase/reductase superfamily of enzymes. Indeed, its active site is reminiscent to that observed for UDP-galactose 4-epimerase, an enzyme that plays a key role in galactose metabolism. Unlike UDP-galactose 4-epimerase where the conversion of configuration occurs about C-4 of the UDP-glucose or UDP-galactose substrates, in the reaction catalyzed by tyvelose epimerase, the inversion of stereochemistry occurs at C-2. On the basis of the observed binding mode for CDP, it is possible to predict the manner in which the substrate, CDP-paratose, and the product, CDP-tyvelose, might be accommodated within the active site of tyvelose epimerase.

About this Structure

1ORR is a Single protein structure of sequence from Salmonella typhi. Full crystallographic information is available from OCA.

Reference

High resolution x-ray structure of tyvelose epimerase from Salmonella typhi., Koropatkin NM, Liu HW, Holden HM, J Biol Chem. 2003 Jun 6;278(23):20874-81. Epub 2003 Mar 17. PMID:12642575 Page seeded by OCA on Sat May 3 04:12:13 2008

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