Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1G9R

CRYSTAL STRUCTURE OF GALACTOSYLTRANSFERASE LGTC IN COMPLEX WITH MN AND UDP-2F-GALACTOSE

Summary for 1G9R
Entry DOI10.2210/pdb1g9r/pdb
Related1GA8
DescriptorGLYCOSYL TRANSFERASE, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE-2-DEOXY-2-FLUOROGALACTOSE, ... (5 entities in total)
Functional Keywordsalpha-beta structure, transferase
Biological sourceNeisseria meningitidis
Total number of polymer chains1
Total formula weight36794.29
Authors
Persson, K.,Hoa, D.L.,Diekelmann, M.,Wakarchuk, W.W.,Withers, S.G.,Strynadka, N.C.J. (deposition date: 2000-11-27, release date: 2001-02-14, Last modification date: 2024-10-30)
Primary citationPersson, K.,Ly, H.D.,Dieckelmann, M.,Wakarchuk, W.W.,Withers, S.G.,Strynadka, N.C.
Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs.
Nat.Struct.Biol., 8:166-175, 2001
Cited by
PubMed Abstract: Many bacterial pathogens express lipooligosaccharides that mimic human cell surface glycoconjugates, enabling them to attach to host receptors and to evade the immune response. In Neisseria meningitidis, the galactosyltransferase LgtC catalyzes a key step in the biosynthesis of lipooligosaccharide structure by transferring alpha-d-galactose from UDP-galactose to a terminal lactose. The product retains the configuration of the donor sugar glycosidic bond; LgtC is thus a retaining glycosyltranferase. We report the 2 A crystal structures of the complex of LgtC with manganese and UDP 2-deoxy-2-fluoro-galactose (a donor sugar analog) in the presence and absence of the acceptor sugar analog 4'-deoxylactose. The structures, together with results from site-directed mutagenesis and kinetic analysis, give valuable insights into the unique catalytic mechanism and, as the first structure of a glycosyltransferase in complex with both the donor and acceptor sugars, provide a starting point for inhibitor design.
PubMed: 11175908
DOI: 10.1038/84168
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

245011

数据于2025-11-19公开中

PDB statisticsPDBj update infoContact PDBjnumon