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2pa7

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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==
==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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<StructureSection load='2pa7' size='340' side='right' caption='[[2pa7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='2pa7' size='340' side='right'caption='[[2pa7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2pa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aneth Aneth]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PA7 FirstGlance]. <br>
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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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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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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</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pae|2pae]], [[2pak|2pak]], [[2pam|2pam]]</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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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fdtA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=143495 ANETH])</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=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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pa7 OCA], [http://pdbe.org/2pa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pa7 RCSB], [http://www.ebi.ac.uk/pdbsum/2pa7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pa7 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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:17459872<ref>PMID:17459872</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2pa7" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aneth]]
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[[Category: Aneurinibacillus thermoaerophilus]]
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[[Category: Davis, M L]]
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[[Category: Large Structures]]
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[[Category: Holden, H M]]
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[[Category: Davis ML]]
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[[Category: Thoden, J B]]
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[[Category: Holden HM]]
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[[Category: Deoxysugar biosynthesis]]
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[[Category: Thoden JB]]
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[[Category: Isomerase]]
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[[Category: Ketoisomerase]]
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[[Category: S-layer biosynthesis]]
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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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