6FZK

NMR structure of UB2H, regulatory domain of PBP1b from E. coli

6FZK の概要

• エントリーDOI: 10.2210/pdb6fzk/pdb
• 関連するPDBエントリー: 3FWL 5HLA 5HLB 5HLD
• NMR情報: BMRB: 34246
• 分子名称: Penicillin-binding protein 1B (1 entity in total)
• 機能のキーワード: ub2h domain of pbp1b, regulatory domain, transferase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13183.97

構造登録者

Simorre, J.P.,Maya Martinez, R.C.,Bougault, C.,Egan, A.J.F.,Vollmer, W. (登録日: 2018-03-15, 公開日: 2019-02-20, 最終更新日: 2024-06-19)

主引用文献

Egan, A.J.F.,Maya-Martinez, R.,Ayala, I.,Bougault, C.M.,Banzhaf, M.,Breukink, E.,Vollmer, W.,Simorre, J.P.
Induced conformational changes activate the peptidoglycan synthase PBP1B.
Mol. Microbiol., 110:335-356, 2018

PubMed Abstract: Bacteria surround their cytoplasmic membrane with an essential, stress-bearing peptidoglycan (PG) layer consisting of glycan chains linked by short peptides into a mesh-like structure. Growing and dividing cells expand their PG layer using inner-membrane anchored PG synthases, including Penicillin-binding proteins (PBPs), which participate in dynamic protein complexes to facilitate cell wall growth. In Escherichia coli, and presumably other Gram-negative bacteria, growth of the mainly single layered PG is regulated by outer membrane-anchored lipoproteins. The lipoprotein LpoB is required to activate PBP1B, which is a major, bi-functional PG synthase with glycan chain polymerising (glycosyltransferase) and peptide cross-linking (transpeptidase) activities. In this work we show how the binding of LpoB to the regulatory UB2H domain of PBP1B activates both activities. Binding induces structural changes in the UB2H domain, which transduce to the two catalytic domains by distinct allosteric pathways. We also show how an additional regulator protein, CpoB, is able to selectively modulate the TPase activation by LpoB without interfering with GTase activation.

PubMed: 30044025
DOI: 10.1111/mmi.14082

実験手法

SOLUTION NMR