5DCC

X-RAY CRYSTAL STRUCTURE OF a TEBIPENEM ADDUCT OF L,D TRANSPEPTIDASE 2 FROM MYCOBACTERIUM TUBERCULOSIS

Summary for 5DCC

• Entry DOI: 10.2210/pdb5dcc/pdb
• Related: 3TUR 5DC2 5DH7
• Descriptor: L,D-transpeptidase 2, (4S)-4-methyl-2,5,7-trioxoheptanoic acid, SULFATE ION, ... (8 entities in total)
• Functional Keywords: l, d -transpeptidase, carbapenems tebipenem-adduct, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 79323.56

Authors

Pan, Y.,Basta, L.,Lamichhane, G.,Bianchet, M.A. (deposition date: 2015-08-23, release date: 2016-09-28, Last modification date: 2024-10-23)

Primary citation

Bianchet, M.A.,Pan, Y.H.,Basta, L.A.B.,Saavedra, H.,Lloyd, E.P.,Kumar, P.,Mattoo, R.,Townsend, C.A.,Lamichhane, G.
Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase LdtMt2 by biapenem and tebipenem.
BMC Biochem., 18:8-8, 2017

PubMed Abstract: The carbapenem subclass of β-lactams is among the most potent antibiotics available today. Emerging evidence shows that, unlike other subclasses of β-lactams, carbapenems bind to and inhibit non-classical transpeptidases (L,D-transpeptidases) that generate 3 → 3 linkages in bacterial peptidoglycan. The carbapenems biapenem and tebipenem exhibit therapeutically valuable potencies against Mycobacterium tuberculosis (Mtb).

PubMed: 28545389
DOI: 10.1186/s12858-017-0082-4

Experimental method

X-RAY DIFFRACTION (2.451 Å)