1orr

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[[Image:1orr.jpg|left|200px]]<br /><applet load="1orr" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1orr, resolution 1.50&Aring;" />
 
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'''Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP'''<br />
 
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==Overview==
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==Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP==
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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.
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<StructureSection load='1orr' size='340' side='right'caption='[[1orr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1orr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhi Salmonella enterica subsp. enterica serovar Typhi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ORR FirstGlance]. <br>
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1ORR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhi Salmonella typhi] with <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=CDP:'>CDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORR OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1orr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1orr OCA], [https://pdbe.org/1orr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1orr RCSB], [https://www.ebi.ac.uk/pdbsum/1orr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1orr ProSAT]</span></td></tr>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12642575 12642575]
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</table>
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[[Category: Salmonella typhi]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/RFBE_SALTI RFBE_SALTI] Catalyzes the isomeration of CDP-paratose to CDP-tyvelose.
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[[Category: Holden, H M.]]
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== Evolutionary Conservation ==
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[[Category: Koropatkin, N M.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Liu, H.]]
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Check<jmol>
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[[Category: CDP]]
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<jmolCheckbox>
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[[Category: NAD]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1orr_consurf.spt"</scriptWhenChecked>
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[[Category: rossmann fold]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: short-chain dehydrogenase/reductase]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:00 2008''
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1orr ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhi]]
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[[Category: Holden HM]]
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[[Category: Koropatkin NM]]
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[[Category: Liu H]]

Current revision

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

PDB ID 1orr

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