6H4D

Crystal structure of RsgA from Pseudomonas aeruginosa

6H4D の概要

• エントリーDOI: 10.2210/pdb6h4d/pdb
• 分子名称: Small ribosomal subunit biogenesis GTPase RsgA, ZINC ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: cpgtpase, ribosome maturation factor, yjeq, rna binding protein
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37637.78

構造登録者

Rocchio, S.,Santorelli, D.,Travaglini-Allocatelli, C.,Federici, L.,Di Matteo, A. (登録日: 2018-07-20, 公開日: 2019-06-26, 最終更新日: 2024-01-17)

主引用文献

Rocchio, S.,Santorelli, D.,Rinaldo, S.,Franceschini, M.,Malatesta, F.,Imperi, F.,Federici, L.,Travaglini-Allocatelli, C.,Di Matteo, A.
Structural and functional investigation of the Small Ribosomal Subunit Biogenesis GTPase A (RsgA) from Pseudomonas aeruginosa.
Febs J., 286:4245-4260, 2019

PubMed Abstract: The Small Ribosomal Subunit Biogenesis GTPase A (RsgA) is a bacterial assembly factor involved in the late stages of the 30S subunit maturation. It is a multidomain GTPase in which the central circularly permutated GTPase domain is flanked by an OB domain and a Zn-binding domain. All three domains participate in the interaction with the 30S particle thus ensuring an efficient coupling between catalytic activity and biological function. In vivo studies suggested the relevance of rsgA in bacterial growth and cellular viability, but other pleiotropic roles of RsgA are also emerging. Here, we report the 3D structure of RsgA from Pseudomonas aeruginosa (PaRsgA) in the GDP-bound form. We also report a biophysical and biochemical characterization of the protein in both the GDP-bound and its nucleotide-free form. In particular, we report a kinetic analysis of the RsgA binding to GTP and GDP. We found that PaRsgA is able to bind both nucleotides with submicromolar affinity. The higher affinity towards GDP (K  = 0.011 μm) with respect to GTP (K  = 0.16 μm) is mainly ascribed to a smaller GDP dissociation rate. Our results confirm that PaRsgA, like most other GTPases, has a weak intrinsic enzymatic activity (k  = 0.058 min ). Finally, the biological role of RsgA in P. aeruginosa was investigated, allowing us to conclude that rsgA is dispensable for P. aeruginosa growth but important for drug resistance and virulence in an animal infection model. DATABASES: Coordinates and structure factors for the protein structure described in this manuscript have been deposited in the Protein Data Bank (https://www.rcsb.org) with the accession code 6H4D.

PubMed: 31199072
DOI: 10.1111/febs.14959

実験手法

X-RAY DIFFRACTION (2.9 Å)