8I1W

The asymmetric structure of homodimeric E. coli TrpRS bound with tryptophanyl adenylate at one of its two active pockets

Summary for 8I1W

Entry DOI	10.2210/pdb8i1w/pdb
Descriptor	Tryptophan--tRNA ligase, SULFATE ION, TRYPTOPHANYL-5'AMP, ... (4 entities in total)
Functional Keywords	homodimer, asymmetric conformation, intermediate product, half-of-the-sites reactivity, aminoacyl-trna synthetase, ligase
Biological source	Escherichia coli K-12
Total number of polymer chains	2
Total formula weight	77665.16
Authors	Xiang, M.,Zhou, H. (deposition date: 2023-01-13, release date: 2023-04-12, Last modification date: 2023-06-07)
Primary citation	Xiang, M.,Xia, K.,Chen, B.,Luo, Z.,Yu, Y.,Jiang, L.,Zhou, H. An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening. Nucleic Acids Res., 51:4637-4649, 2023 Cited by PubMed: 37070195 DOI: 10.1093/nar/gkad278 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation