2pak
From Proteopedia
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|PDB= 2pak |SIZE=350|CAPTION= <scene name='initialview01'>2pak</scene>, resolution 2.40Å | |PDB= 2pak |SIZE=350|CAPTION= <scene name='initialview01'>2pak</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=TYD:THYMIDINE-5 | + | |LIGAND= <scene name='pdbligand=TYD:THYMIDINE-5'- DIPHOSPHATE'>TYD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= fdtA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=143495 Aneurinibacillus thermoaerophilus]) | |GENE= fdtA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=143495 Aneurinibacillus thermoaerophilus]) | ||
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[[Category: s-layer biosynthesis]] | [[Category: s-layer biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:38:00 2008'' |
Revision as of 13:38, 23 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Gene: | fdtA (Aneurinibacillus thermoaerophilus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a H51N mutant dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from Aneurinibacillus thermoaerophilus complexed with TDP
Overview
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.
About this Structure
2PAK is a Single protein structure of sequence from Aneurinibacillus thermoaerophilus. Full crystallographic information is available from OCA.
Reference
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
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