1IIR

Crystal Structure of UDP-glucosyltransferase GtfB

Summary for 1IIR

• Entry DOI: 10.2210/pdb1iir/pdb
• Descriptor: glycosyltransferase GtfB, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, rossmann fold, transferase
• Biological source: Amycolatopsis orientalis
• Total number of polymer chains: 1
• Total formula weight: 43922.11

Authors

Mulichak, A.M.,Losey, H.C.,Walsh, C.T.,Garavito, R.M. (deposition date: 2001-04-24, release date: 2001-07-18, Last modification date: 2024-02-07)

Primary citation

Mulichak, A.M.,Losey, H.C.,Walsh, C.T.,Garavito, R.M.
Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics.
Structure, 9:547-557, 2001

PubMed Abstract: Members of the vancomycin group of glycopeptide antibiotics have an oxidatively crosslinked heptapeptide scaffold decorated at the hydroxyl groups of 4-OH-Phegly4 or beta-OH-Tyr6 with mono- (residue 6) or disaccharides (residue 4). The disaccharide in vancomycin itself is L-vancosamine-1,2-glucose, and in chloroeremomycin it is L-4-epi-vancosamine-1,2-glucose. The sugars and their substituents play an important role in efficacy, particularly against vancomycin-resistant pathogenic enterococci.

PubMed: 11470430
DOI: 10.1016/S0969-2126(01)00616-5

Experimental method

X-RAY DIFFRACTION (1.8 Å)