7QYS

Crystal structure of RimK from Pseudomonas syringae DC3000

7QYS の概要

• エントリーDOI: 10.2210/pdb7qys/pdb
• 分子名称: Probable alpha-L-glutamate ligase, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: atp-grasp fold, glutamate ligase, ribosomal modification, ligase
• 由来する生物種: Pseudomonas syringae pv. tomato str. DC3000
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 545424.27

構造登録者

Thompson, C.M.A.,Little, R.H.,Stevenson, C.E.M.,Lawson, D.M.,Malone, J.G. (登録日: 2022-01-29, 公開日: 2022-10-05, 最終更新日: 2024-02-07)

主引用文献

Thompson, C.M.A.,Little, R.H.,Stevenson, C.E.M.,Lawson, D.M.,Malone, J.G.
Structural insights into the mechanism of adaptive ribosomal modification by Pseudomonas RimK.
Proteins, 91:300-314, 2023

PubMed Abstract: Bacteria are equipped with a diverse set of regulatory tools that allow them to quickly adapt to their environment. The RimK system allows for Pseudomonas spp. to adapt through post-transcriptional regulation by altering the ribosomal subunit RpsF. RimK is found in a wide range of bacteria with a conserved amino acid sequence, however, the genetic context and the role of this protein is highly diverse. By solving and comparing the structures of RimK homologs from two related but functionally divergent systems, we uncovered key structural differences that likely contribute to the different activity levels of each of these homologs. Moreover, we were able to clearly resolve the active site of this protein for the first time, resolving binding of the glutamate substrate. This work advances our understanding of how subtle differences in protein sequence and structure can have profound effects on protein activity, which can in turn result in widespread mechanistic changes.

PubMed: 36134899
DOI: 10.1002/prot.26429

実験手法

X-RAY DIFFRACTION (2.9 Å)