2pa7

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(New page: 200px<br /><applet load="2pa7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pa7, resolution 1.5&Aring;" /> '''Structure of Wild-Typ...)
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[[Image:2pa7.gif|left|200px]]<br /><applet load="2pa7" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pa7, resolution 1.5&Aring;" />
 
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'''Structure of Wild-Type dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from Aneurinibacillus thermoaerophilus in complex with TDP'''<br />
 
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==Overview==
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==Structure of Wild-Type dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from Aneurinibacillus thermoaerophilus in complex with TDP==
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The repeating unit of the glycan chain in the S-layer of the bacterium, Aneurinibacillus thermoaerophilus L420-91(T) is composed of four, alpha-d-rhamnose molecules and two, 3-acetamido-3,6-dideoxy-alpha-d-galactose moieties (abbreviated as, Fucp3NAc). Formation of the glycan layer requires nucleotide-activated, sugars as the donor molecules. Whereas the enzymes involved in the, synthesis of GDP-rhamnose have been well characterized, less is known, regarding the structures and enzymatic mechanisms of the enzymes required, for the production of dTDP-Fucp3NAc. One of the enzymes involved in the, biosynthesis of dTDP-Fucp3NAc is a 3,4-ketoisomerase, hereafter referred, to as FdtA. Here we describe the first three-dimensional structure of this, sugar isomerase complexed with dTDP and solved to 1.5 A resolution. The, FdtA dimer assumes an almost jellyfish-like appearance with the sole, alpha-helices representing the tentacles. Formation of the FdtA dimer, represents a classical example of domain swapping whereby beta-strands 2, and 3 from one subunit form part of a beta-sheet in the second subunit., The active site architecture of FdtA is characterized by a cluster of, three histidine residues, two of which, His(49) and His(51), appear to be, strictly conserved in the amino acid sequences deposited to date., Site-directed mutagenesis experiments, enzymatic assays, and x-ray, crystallographic analyses suggest that His(49) functions as an active site, base.
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<StructureSection load='2pa7' size='340' side='right'caption='[[2pa7]], [[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'>[[2pa7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aneurinibacillus_thermoaerophilus Aneurinibacillus thermoaerophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PA7 FirstGlance]. <br>
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2PA7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aneurinibacillus_thermoaerophilus Aneurinibacillus thermoaerophilus] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=TYD:'>TYD</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PA7 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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=2pa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pa7 OCA], [https://pdbe.org/2pa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pa7 RCSB], [https://www.ebi.ac.uk/pdbsum/2pa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pa7 ProSAT]</span></td></tr>
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The X-ray Structure of dTDP-4-Keto-6-deoxy-D-glucose-3,4-ketoisomerase., Davis ML, Thoden JB, Holden HM, J Biol Chem. 2007 Jun 29;282(26):19227-36. Epub 2007 Apr 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17459872 17459872]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FDTA_ANETH FDTA_ANETH] Mediates the isomerization of dTDP-6-deoxy-D-xylohex-4-ulose into dTDP-6-deoxy-D-xylohex-3-ulose in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose, a glycan chain of the S-layer.<ref>PMID:12740380</ref> <ref>PMID:17459872</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pa/2pa7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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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=2pa7 ConSurf].
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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>
[[Category: Aneurinibacillus thermoaerophilus]]
[[Category: Aneurinibacillus thermoaerophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Davis, M.L.]]
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[[Category: Davis ML]]
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[[Category: Holden, H.M.]]
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[[Category: Holden HM]]
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[[Category: Thoden, J.B.]]
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[[Category: Thoden JB]]
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[[Category: CL]]
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[[Category: EDO]]
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[[Category: TYD]]
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[[Category: deoxysugar biosynthesis]]
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[[Category: ketoisomerase]]
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[[Category: s-layer biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:38:12 2008''
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Current revision

Structure of Wild-Type dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from Aneurinibacillus thermoaerophilus in complex with TDP

PDB ID 2pa7

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