7LQ6

CryoEM structure of Escherichia coli PBP1b

Summary for 7LQ6

• Entry DOI: 10.2210/pdb7lq6/pdb
• EMDB information: 23482
• Descriptor: Penicillin-binding protein 1B (1 entity in total)
• Functional Keywords: penicillin binding protein, glycosyltransferase, transpeptidase, transferase, hydrolase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 1
• Total formula weight: 83280.35

Authors

Caveney, N.A.,Workman, S.D.,Yan, R.,Atkinson, C.E.,Yu, Z.,Strynadka, N.C.J. (deposition date: 2021-02-13, release date: 2021-05-26, Last modification date: 2024-03-06)

Primary citation

Caveney, N.A.,Workman, S.D.,Yan, R.,Atkinson, C.E.,Yu, Z.,Strynadka, N.C.J.
CryoEM structure of the antibacterial target PBP1b at 3.3 angstrom resolution.
Nat Commun, 12:2775-2775, 2021

PubMed Abstract: The pathway for the biosynthesis of the bacterial cell wall is one of the most prolific antibiotic targets, exemplified by the widespread use of β-lactam antibiotics. Despite this, our structural understanding of class A penicillin binding proteins, which perform the last two steps in this pathway, is incomplete due to the inherent difficulty in their crystallization and the complexity of their substrates. Here, we determine the near atomic resolution structure of the 83 kDa class A PBP from Escherichia coli, PBP1b, using cryogenic electron microscopy and a styrene maleic acid anhydride membrane mimetic. PBP1b, in its apo form, is seen to exhibit a distinct conformation in comparison to Moenomycin-bound crystal structures. The work herein paves the way for the use of cryoEM in structure-guided antibiotic development for this notoriously difficult to crystalize class of proteins and their complex substrates.

PubMed: 33986273
DOI: 10.1038/s41467-021-23063-6

Experimental method

ELECTRON MICROSCOPY (3.28 Å)