8E2C

N-terminal domain of S. aureus GpsB in complex with PBP4 fragment

8E2C の概要

• エントリーDOI: 10.2210/pdb8e2c/pdb
• 分子名称: Cell cycle protein GpsB, PBP4 (3 entities in total)
• 機能のキーワード: peptidoglycan, pbp, pbp4, mrsa, gpsb, pbp2a cell wall, transpeptidase, b-lactam, gram-positive, sporulation, peptide binding protein, cell division, bacterial cell division, diviva, divisome
• 由来する生物種: Staphylococcus aureus subsp. aureus COL; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 17650.09

構造登録者

Sacco, M.,Chen, Y. (登録日: 2022-08-14, 公開日: 2023-08-09, 最終更新日: 2024-05-08)

主引用文献

Sacco, M.D.,Hammond, L.R.,Noor, R.E.,Bhattacharya, D.,McKnight, L.J.,Madsen, J.J.,Zhang, X.,Butler, S.G.,Kemp, M.T.,Jaskolka-Brown, A.C.,Khan, S.J.,Gelis, I.,Eswara, P.,Chen, Y.
Staphylococcus aureus FtsZ and PBP4 bind to the conformationally dynamic N-terminal domain of GpsB.
Elife, 13:-, 2024

PubMed Abstract: In the Firmicutes phylum, GpsB is a membrane associated protein that coordinates peptidoglycan synthesis with cell growth and division. Although GpsB has been studied in several bacteria, the structure, function, and interactome of GpsB is largely uncharacterized. To address this knowledge gap, we solved the crystal structure of the N-terminal domain of GpsB, which adopts an atypical, asymmetric dimer, and demonstrates major conformational flexibility that can be mapped to a hinge region formed by a three-residue insertion exclusive to . When this three-residue insertion is excised, its thermal stability increases, and the mutant no longer produces a previously reported lethal phenotype when overexpressed in . In , we show that these hinge mutants are less functional and speculate that the conformational flexibility imparted by the hinge region may serve as a dynamic switch to fine-tune the function of the GpsB complex and/or to promote interaction with its various partners. Furthermore, we provide the first biochemical, biophysical, and crystallographic evidence that the N-terminal domain of GpsB binds not only PBP4, but also FtsZ, through a conserved recognition motif located on their C-termini, thus coupling peptidoglycan synthesis to cell division. Taken together, the unique structure of GpsB and its direct interaction with FtsZ/PBP4 provide deeper insight into the central role of GpsB in cell division.

PubMed: 38639993
DOI: 10.7554/eLife.85579

実験手法

X-RAY DIFFRACTION (2.4 Å)