CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution.
CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution.
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DOI:
10.1038/s41467-021-23063-6
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发表时间:
2021-05-13
影响因子:
16.6
通讯作者:
Strynadka NCJ
中科院分区:
文献类型:
--
作者:
Caveney NA;Workman SD;Yan R;Atkinson CE;Yu Z;Strynadka NCJ
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. Our structural understanding of class A penicillin binding proteins is incomplete due to the difficulty in their crystallization and the complexity of their substrates. Here, authors determine the structure of the 83 kDa class A PBP from Escherichia coli, PBP1b, using cryogenic electron microscopy and a styrene maleic acid anhydride membrane mimetic.
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通讯作者:
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影响因子:
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DOI:
10.1073/pnas.1400376111
发表时间:
2014-06-03
影响因子:
11.1
作者:
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通讯作者:
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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
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通讯作者:
Cowtan, K