4B0S

Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ATP

4B0S の概要

• エントリーDOI: 10.2210/pdb4b0s/pdb
• 関連するPDBエントリー: 4B0R 4B0T
• 分子名称: DEAMIDASE-DEPUPYLASE DOP, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, pupylation, prokaryotic ubiquitin-like protein, proteasome
• 由来する生物種: ACIDOTHERMUS CELLULOLYTICUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57682.97

構造登録者

Ozcelik, D.,Barandun, J.,Schmitz, N.,Sutter, M.,Guth, E.,Damberger, F.F.,Allain, F.H.-T.,Ban, N.,Weber-Ban, E. (登録日: 2012-07-04, 公開日: 2012-09-12, 最終更新日: 2024-05-08)

主引用文献

Ozcelik, D.,Barandun, J.,Schmitz, N.,Sutter, M.,Guth, E.,Damberger, F.F.,Allain, F.H.-T.,Ban, N.,Weber-Ban, E.
Structures of Pup Ligase Pafa and Depupylase Dop from the Prokaryotic Ubiquitin-Like Modification Pathway.
Nat.Commun., 3:1014-, 2012

PubMed Abstract: Pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination. Here we report the crystal structures of the modification enzymes involved in this pathway, the prokaryotic ubiquitin-like protein (Pup) ligase PafA and the depupylase/deamidase Dop. Both feature a larger amino-terminal domain consisting of a central β-sheet packed against a cluster of helices, a fold characteristic for carboxylate-amine ligases, and a smaller C-terminal domain unique to PafA/Dop members. The active site is located on the concave surface of the β-sheet with the nucleotide bound in a deep pocket. A conserved groove leading into the active site could have a role in Pup-binding. Nuclear magnetic resonance and biochemical experiments determine the region of Pup that interacts with PafA and Dop. Structural data and mutational studies identify crucial residues for the catalysis of both enzymes.

PubMed: 22910360
DOI: 10.1038/NCOMMS2009

実験手法

X-RAY DIFFRACTION (2.85 Å)