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-Structure paper
タイトル | CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 2775, Year 2021 |
掲載日 | 2021年5月13日 |
著者 | Nathanael A Caveney / Sean D Workman / Rui Yan / Claire E Atkinson / Zhiheng Yu / Natalie C J Strynadka / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:33986273 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.28 Å |
構造データ | EMDB-23482, PDB-7lq6: |
由来 |
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キーワード | TRANSFERASE / HYDROLASE / Penicillin binding protein / glycosyltransferase / transpeptidase |