6RRM

Crystal structure of LdtMt2 from Mycobacterium tuberculosis bound to Ebselen

Summary for 6RRM

Entry DOI	10.2210/pdb6rrm/pdb
Descriptor	L,D-transpeptidase 2, AMMONIUM ION, GLYCEROL, ... (6 entities in total)
Functional Keywords	beta lactmase, antibiotic resistance, tuberculosis, antimicrobial protein
Biological source	Mycobacterium tuberculosis CDC1551
Total number of polymer chains	2
Total formula weight	76847.15
Authors	Brem, J.,Lohans, C.,Schofield, C. (deposition date: 2019-05-20, release date: 2019-08-14, Last modification date: 2024-11-06)
Primary citation	de Munnik, M.,Lohans, C.T.,Lang, P.A.,Langley, G.W.,Malla, T.R.,Tumber, A.,Schofield, C.J.,Brem, J. Targeting the Mycobacterium tuberculosis transpeptidase LdtMt2with cysteine-reactive inhibitors including ebselen. Chem.Commun.(Camb.), 55:10214-10217, 2019 Cited by PubMed Abstract: The l,d-transpeptidases (Ldts) are promising antibiotic targets for treating tuberculosis. We report screening of cysteine-reactive inhibitors against LdtMt2 from Mycobacterium tuberculosis. Structural studies on LdtMt2 with potent inhibitor ebselen reveal opening of the benzisoselenazolone ring by a nucleophilic cysteine, forming a complex involving extensive hydrophobic interactions with a substrate-binding loop. PubMed: 31380528 DOI: 10.1039/c9cc04145a PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.64 Å)

Structure validation