2QIV

Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase

Summary for 2QIV

• Entry DOI: 10.2210/pdb2qiv/pdb
• Related: 2QIA
• Descriptor: UDP-N-acetylglucosamine acyltransferase, uridine-5'-diphosphate-3-O-(R-3-hydroxydecanoyl)-N-acetyl-D-glucosamine (3 entities in total)
• Functional Keywords: left-handed parallel beta helix; protein lipid recognition, transferase
• Biological source: Escherichia coli K12
• Cellular location: Cytoplasm: P0A722
• Total number of polymer chains: 1
• Total formula weight: 28894.62

Authors

Williams, A.H.,Raetz, C.R.H. (deposition date: 2007-07-05, release date: 2007-10-02, Last modification date: 2024-02-21)

• Primary citation: Williams, A.H.,Raetz, C.R.H.; Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase; Proc.Natl.Acad.Sci.Usa, 104:13543-13550, 2007; PubMed: 17698807; DOI: 10.1073/pnas.0705833104

Experimental method

X-RAY DIFFRACTION (1.85 Å)