2pa7

<table><tr><td colspan='2'>[[2pa7]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2PA7 FirstGlance]. <br>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pae|2pae]], [[2pak|2pak]], [[2pam|2pam]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fdtA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=143495 ANETH])</td></tr>

[[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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2pa7" style="background-color:#fffaf0;"></div>

[[Category: Aneth]]

[[Category: Davis, M L]]

[[Category: Holden, H M]]

[[Category: Thoden, J B]]

[[Category: S-layer biosynthesis]]