5CTN

Structure of BPu1 beta-lactamase

Summary for 5CTN

• Entry DOI: 10.2210/pdb5ctn/pdb
• Related: 5CTM
• Descriptor: Beta-lactamase, (2~{S},3~{R})-3-methyl-2-[(2~{S},3~{R})-3-oxidanyl-1-oxidanylidene-butan-2-yl]-4-[(3~{S},5~{S})-5-[(sulfamoylamino)meth yl]pyrrolidin-3-yl]sulfanyl-3,4-dihydro-2~{H}-pyrrole-5-carboxylic acid, CITRATE ANION, ... (4 entities in total)
• Functional Keywords: hydrolase, beta-lactamase
• Biological source: Bacillus pumilus
• Total number of polymer chains: 2
• Total formula weight: 55662.45

Authors

Smith, C.A.,Vakulenko, S.B. (deposition date: 2015-07-24, release date: 2015-11-25, Last modification date: 2024-10-16)

Primary citation

Toth, M.,Antunes, N.T.,Stewart, N.K.,Frase, H.,Bhattacharya, M.,Smith, C.A.,Vakulenko, S.B.
Class D beta-lactamases do exist in Gram-positive bacteria.
Nat.Chem.Biol., 12:9-14, 2016

PubMed Abstract: Production of β-lactamases of one of four molecular classes (A, B, C and D) is the major mechanism of bacterial resistance to β-lactams, the largest class of antibiotics, which have saved countless lives since their inception 70 years ago. Although several hundred efficient class D enzymes have been identified in Gram-negative pathogens over the last four decades, none have been reported in Gram-positive bacteria. Here we demonstrate that efficient class D β-lactamases capable of hydrolyzing a wide array of β-lactam substrates are widely disseminated in various species of environmental Gram-positive organisms. Class D enzymes of Gram-positive bacteria have a distinct structural architecture and employ a unique substrate-binding mode that is quite different from that of all currently known class A, C and D β-lactamases. These enzymes thus constitute a previously unknown reservoir of novel antibiotic-resistance enzymes.

PubMed: 26551395
DOI: 10.1038/nchembio.1950

Experimental method

X-RAY DIFFRACTION (1.35 Å)