4yfy

X-ray structure of the Viof N-formyltransferase from Providencia alcalifaciens O30 in complex with THF and TDP-Qui4N

spinqualitylabelsall models 4yfy, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yfy is a 2 chain structure with sequence from Providencia alcalifaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: 0FX, 1YJ, CL, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M9P0Q2_9GAMM Publication Abstract from PubMed The existence of N-formylated sugars in the O-antigens of Gram-negative bacteria has been known since the middle 1980s, but only recently have the biosynthetic pathways for their production been reported. In these pathways, glucose-1-phosphate is first activated by attachment to a dTMP moiety. This step is followed by a dehydration reaction and an amination. The last step in these pathways is catalyzed by N-formyltransferases that utilize N10 -formyltetrahydrofolate as the carbon source. Here we describe the three-dimensional structure of one of these N-formyltransferases, namely VioF from Providencia alcalifaciens O30. Specifically, this enzyme catalyzes the conversion of dTDP-4-amino-6-deoxyglucose (dTDP-Qui4N) to dTDP-4,6-dideoxy-4-formamido-d-glucose (dTDP-Qui4NFo). For this analysis, the structure of VioF was solved to 1.9 A resolution in both its apoform and in complex with tetrahydrofolate and dTDP-Qui4N. The crystals used in the investigation belonged to the space group R32 and demonstrated reticular merohedral twinning. The overall catalytic core of the VioF subunit is characterized by a six stranded mixed beta-sheet flanked on one side by three alpha-helices and on the other side by mostly random coil. This N-terminal domain is followed by an alpha-helix and a beta-hairpin that form the subunit:subunit interface. The active site of the enzyme is shallow and solvent-exposed. Notably, the pyranosyl moiety of dTDP-Qui4N is positioned into the active site by only one hydrogen bond provided by Lys 77. Comparison of the VioF model to that of a previously determined N-formyltransferase suggests that substrate specificity is determined by interactions between the protein and the pyrophosphoryl group of the dTDP-sugar substrate. This article is protected by copyright. All rights reserved. Molecular Structure of an N-formyltransferase from Providencia alcalifaciens O30.,Genthe NA, Thoden JB, Benning MM, Holden HM Protein Sci. 2015 Mar 9. doi: 10.1002/pro.2675. PMID:25752909 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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