5U1Z
X-ray structure of the WlarG aminotransferase, apo form, from Campylobacter jejune
Summary for 5U1Z
Entry DOI | 10.2210/pdb5u1z/pdb |
Related | 5U20 5U21 5U23 5U24 |
Descriptor | Putative aminotransferase, CHLORIDE ION, SODIUM ION, ... (4 entities in total) |
Functional Keywords | aminotransferase, plp, lipooligosaccharide, transferase |
Biological source | Campylobacter jejuni |
Total number of polymer chains | 4 |
Total formula weight | 176330.46 |
Authors | Holden, H.M.,Thoden, J.B.,Dow, G.T.,Gilbert, M. (deposition date: 2016-11-29, release date: 2017-01-11, Last modification date: 2023-10-04) |
Primary citation | Dow, G.T.,Gilbert, M.,Thoden, J.B.,Holden, H.M. Structural investigation on WlaRG from Campylobacter jejuni: A sugar aminotransferase. Protein Sci., 26:586-599, 2017 Cited by PubMed Abstract: Campylobacter jejuni is a Gram-negative bacterium that represents a leading cause of human gastroenteritis worldwide. Of particular concern is the link between C. jejuni infections and the subsequent development of Guillain-Barré syndrome, an acquired autoimmune disorder leading to paralysis. All Gram-negative bacteria contain complex glycoconjugates anchored to their outer membranes, but in most strains of C. jejuni, this lipoglycan lacks the O-antigen repeating units. Recent mass spectrometry analyses indicate that the C. jejuni 81116 (Penner serotype HS:6) lipoglycan contains two dideoxyhexosamine residues, and enzymological assay data show that this bacterial strain can synthesize both dTDP-3-acetamido-3,6-dideoxy-d-glucose and dTDP-3-acetamido-3,6-dideoxy-d-galactose. The focus of this investigation is on WlaRG from C. jejuni, which plays a key role in the production of these unusual sugars by functioning as a pyridoxal 5'-phosphate dependent aminotransferase. Here, we describe the first three-dimensional structures of the enzyme in various complexes determined to resolutions of 1.7 Å or higher. Of particular significance are the external aldimine structures of WlaRG solved in the presence of either dTDP-3-amino-3,6-dideoxy-d-galactose or dTDP-3-amino-3,6-dideoxy-d-glucose. These models highlight the manner in which WlaRG can accommodate sugars with differing stereochemistries about their C-4' carbon positions. In addition, we present a corrected structure of WbpE, a related sugar aminotransferase from Pseudomonas aeruginosa, solved to 1.3 Å resolution. PubMed: 28028852DOI: 10.1002/pro.3109 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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