3INR
Structure of UDP-galactopyranose mutase bound to UDP-galactose (oxidized)
Summary for 3INR
| Entry DOI | 10.2210/pdb3inr/pdb |
| Related | 1I8T 1V0J 1WAM 2BI7 2BI8 3GF4 3INT |
| Descriptor | UDP-galactopyranose mutase, FLAVIN-ADENINE DINUCLEOTIDE, GALACTOSE-URIDINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | flavoenzyme, protein-ligand complex, carbohydrate biosynthesis, isomerase, fad, flavoprotein, lipopolysaccharide biosynthesis |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 2 |
| Total formula weight | 93179.59 |
| Authors | Gruber, T.D.,Kiessling, L.L.,Forest, K.T. (deposition date: 2009-08-12, release date: 2009-09-22, Last modification date: 2023-09-06) |
| Primary citation | Gruber, T.D.,Westler, W.M.,Kiessling, L.L.,Forest, K.T. X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin . Biochemistry, 48:9171-9173, 2009 Cited by PubMed Abstract: The flavoenzyme uridine 5'-diphosphate galactopyranose mutase (UGM or Glf) catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose. The latter is a key building block for cell wall construction in numerous pathogens, including Mycobacterium tuberculosis. Mechanistic studies of UGM suggested a novel role for the flavin, and we previously provided evidence that the catalytic mechanism proceeds through a covalent flavin-galactose iminium. Here, we describe 2.3 and 2.5 A resolution X-ray crystal structures of the substrate-bound enzyme in oxidized and reduced forms, respectively. In the latter, C1 of the substrate is 3.6 A from the nucleophilic flavin N5 position. This orientation is consistent with covalent catalysis by flavin. PubMed: 19719175DOI: 10.1021/bi901437v PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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