3Q4I

Crystal structure of CDP-Chase in complex with Gd3+

3Q4I の概要

• エントリーDOI: 10.2210/pdb3q4i/pdb
• 関連するPDBエントリー: 3Q1P
• 分子名称: Phosphohydrolase (MutT/nudix family protein), GADOLINIUM ION (3 entities in total)
• 機能のキーワード: nudix hydrolase, asymmetric dimer, pyrophosphatase, rna exonuclease, cdp-choline pyrophosphatase, hydrolase
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47909.50

構造登録者

Duong-Ly, K.C.,Gabelli, S.B.,Amzel, L.M. (登録日: 2010-12-23, 公開日: 2011-07-13, 最終更新日: 2024-02-21)

主引用文献

Duong-Ly, K.C.,Gabelli, S.B.,Xu, W.,Dunn, C.A.,Schoeffield, A.J.,Bessman, M.J.,Amzel, L.M.
The Nudix Hydrolase CDP-Chase, a CDP-Choline Pyrophosphatase, Is an Asymmetric Dimer with Two Distinct Enzymatic Activities.
J.Bacteriol., 193:3175-3185, 2011

PubMed Abstract: A Nudix enzyme from Bacillus cereus (NCBI RefSeq accession no. NP_831800) catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. Here, we show that in addition, the enzyme has a 3'→5' RNA exonuclease activity. The structure of the free enzyme, determined to a 1.8-Å resolution, shows that the enzyme is an asymmetric dimer. Each monomer consists of two domains, an N-terminal helical domain and a C-terminal Nudix domain. The N-terminal domain is placed relative to the C-terminal domain such as to result in an overall asymmetric arrangement with two distinct catalytic sites: one with an "enclosed" Nudix pyrophosphatase site and the other with a more open, less-defined cavity. Residues that may be important for determining the asymmetry are conserved among a group of uncharacterized Nudix enzymes from Gram-positive bacteria. Our data support a model where CDP-choline hydrolysis is catalyzed by the enclosed Nudix site and RNA exonuclease activity is catalyzed by the open site. CDP-Chase is the first identified member of a novel Nudix family in which structural asymmetry has a profound effect on the recognition of substrates.

PubMed: 21531795
DOI: 10.1128/JB.00089-11

実験手法

X-RAY DIFFRACTION (2.5 Å)