8e77 | pdb_00008e77

rystal structure of Pcryo_0616, the aminotransferase required to synthesize UDP-N-acetyl-3-amino-D-glucosaminuronic acid (UDP-GlcNAc3NA), incomplete with its external aldimine reaction intermediate

spinqualitylabelsall models 8e77, resolution 1.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8e77 is a 1 chain structure with sequence from Psychrobacter cryohalolentis K5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1Å Ligands: EDO, NA, ULP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1QD54_PSYCK Publication Abstract from PubMed Psychrobacter cryohalolentis K5(T) is a Gram negative bacterium first isolated from Siberian permafrost in 2006. It has a complex O-antigen containing l-rhamnose, d-galactose, two diacetamido-sugars, and one triacetamido-sugar. The biosynthetic pathway for one of the diacetamido-sugars, namely 2,3-diacetamido-2,3-dideoxy-alpha-d-glucuronic acid, is presently unknown. Utilizing the published genome sequence of P. cryohalolentis K5(T) , we hypothesized that the genes designated Pcryo_0613, Pcryo_0614, Pcryo_0616, and Pcryo_0615 encode for a UDP-N-acetyl-d-glucosamine 6-dehydrogenase, an NAD(+) -dependent dehydrogenase, a PLP-dependent aminotransferase, and an N-acetyltransferase, respectively, activities of which would be required for the biosynthesis of this unusual carbohydrate. Here we present the cloning, overexpression and purification of these hypothetical proteins. Kinetic data on the enzymes encoded by Pcryo_0613, Pcryo_0614, and Pcryo_0615 confirmed their postulated biochemical activities. In addition, the high resolution X-ray structures of both the internal and external aldimine forms of the aminotransferase were determined to 1.25 A and 1.0 A, respectively. Finally, the three-dimensional architecture of the N-acetyltransferase in complex with its substrate and CoA was solved to 1.8 A resolution. Strikingly, the N-acetyltransferase was shown to adopt a new motif for UDP-sugar binding. The data presented herein provide additional insight into sugar biosynthesis in Gram negative bacteria. This article is protected by copyright. All rights reserved. Investigation of the Enzymes Required for the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-glucuronic acid in Psychrobacter cryohalolentis K5(T).,Hofmeister DL, Seltzner CA, Bockhaus NJ, Thoden JB, Holden HM Protein Sci. 2022 Nov 8:e4502. doi: 10.1002/pro.4502. PMID:36346293 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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