1gfs

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(New page: 200px<br /><applet load="1gfs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gfs, resolution 2.20&Aring;" /> '''GDP-FUCOSE SYNTHETAS...)
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[[Image:1gfs.jpg|left|200px]]<br /><applet load="1gfs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gfs, resolution 2.20&Aring;" />
 
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'''GDP-FUCOSE SYNTHETASE FROM E. COLI'''<br />
 
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==Overview==
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==GDP-FUCOSE SYNTHETASE FROM E. COLI==
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Background:. In all species examined, GDP-fucose is synthesized from, GDP-mannose in a three-step reaction catalyzed by two enzymes, GDP-mannose, 4,6 dehydratase and a dual function 3, 5-epimerase-4-reductase named, GDP-fucose synthetase. In this latter aspect fucose biosynthesis differs, from that of other deoxy and dideoxy sugars, in which the epimerase and, reductase activities are present as separate enzymes. Defects in, GDP-fucose biosynthesis have been shown to affect nodulation in bacteria, stem development in plants, and are associated with the immune defect, leukocyte adhesion deficiency type II in humans. Results:. We have, determined the structure of GDP-fucose synthetase from Escherichia coli at, 2.2 A resolution. The structure of GDP-fucose synthetase is closely, related to that of UDP-galactose 4-epimerase and more distantly to other, members of the short-chain dehydrogenase/reductase family. We have also, determined the structures of the binary complexes of GDP-fucose synthetase, with its substrate NADPH and its product NADP+. The nicotinamide cofactors, bind in the syn and anti conformations, respectively. Conclusions:., GDP-fucose synthetase binds its substrate, NADPH, in the proper, orientation (syn) for transferring the 4-pro-S hydride of the, nicotinamide. We have observed a single binding site in GDP-fucose, synthetase for the second substrate, GDP-4-keto,6-deoxy-mannose. This, implies that both the epimerization and reduction reactions occur at the, same site in the enzyme. As is the case for all members of the short-chain, family of dehydrogenase/reductases, GDP-fucose synthetase retains the, Ser-Tyr-Lys catalytic triad. We propose that this catalytic triad, functions in a mechanistically equivalent manner in both the epimerization, and reduction reactions. Additionally, the X-ray structure has allowed us, to identify other residues that are potentially required for substrate, binding and catalysis.
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<StructureSection load='1gfs' size='340' side='right'caption='[[1gfs]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1gfs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GFS FirstGlance]. <br>
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1GFS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GFS 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]] 2.2&#8491;</td></tr>
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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=1gfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gfs OCA], [https://pdbe.org/1gfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gfs RCSB], [https://www.ebi.ac.uk/pdbsum/1gfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gfs ProSAT]</span></td></tr>
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==Reference==
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</table>
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GDP-fucose synthetase from Escherichia coli: structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site., Somers WS, Stahl ML, Sullivan FX, Structure. 1998 Dec 15;6(12):1601-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9862812 9862812]
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== Function ==
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[[Category: Escherichia coli]]
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[https://www.uniprot.org/uniprot/FCL_ECOLI FCL_ECOLI] Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.<ref>PMID:9473059</ref> <ref>PMID:10480878</ref> <ref>PMID:11021971</ref>
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Somers, W.S.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Stahl, M.L.]]
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Check<jmol>
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[[Category: Sullivan, F.X.]]
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<jmolCheckbox>
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[[Category: epimerase-reductase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/1gfs_consurf.spt"</scriptWhenChecked>
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[[Category: gdp-fucose]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: lipopolysaccharide biosynthesis]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: nadp]]
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</jmolCheckbox>
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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=1gfs ConSurf].
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:01:07 2007''
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Somers WS]]
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[[Category: Stahl ML]]
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[[Category: Sullivan FX]]

Current revision

GDP-FUCOSE SYNTHETASE FROM E. COLI

PDB ID 1gfs

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