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5DS7

2.0 A Structure of CPII, a nitrogen regulatory PII-like protein from Thiomonas intermedia K12, bound AMP

5DS7 の概要
エントリーDOI10.2210/pdb5ds7/pdb
関連するPDBエントリー5DRK
分子名称Nitrogen regulatory protein P-II, ADENOSINE MONOPHOSPHATE, CHLORIDE ION, ... (4 entities in total)
機能のキーワードcarbon regulatory pii protein, cpii, nitrogen regulatory pii protein, nucleotide binding, adp hydrolysis, bicarbonate, acetate binding, metal binding protein
由来する生物種Thiomonas intermedia (strain K12)
タンパク質・核酸の鎖数3
化学式量合計36929.71
構造登録者
Wheatley, N.M.,Ngo, J.,Cascio, D.,Sawaya, M.R.,Yeates, T.O. (登録日: 2015-09-17, 公開日: 2016-09-28, 最終更新日: 2024-03-06)
主引用文献Wheatley, N.M.,Eden, K.D.,Ngo, J.,Rosinski, J.S.,Sawaya, M.R.,Cascio, D.,Collazo, M.,Hoveida, H.,Hubbell, W.L.,Yeates, T.O.
A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein.
J.Mol.Biol., 428:4013-4030, 2016
Cited by
PubMed Abstract: Autotrophic bacteria rely on various mechanisms to increase intracellular concentrations of inorganic forms of carbon (i.e., bicarbonate and CO) in order to improve the efficiency with which they can be converted to organic forms. Transmembrane bicarbonate transporters and carboxysomes play key roles in accumulating bicarbonate and CO, but other regulatory elements of carbon concentration mechanisms in bacteria are less understood. In this study, after analyzing the genomic regions around α-type carboxysome operons, we characterize a protein that is conserved across these operons but has not been previously studied. On the basis of a series of apo- and ligand-bound crystal structures and supporting biochemical data, we show that this protein, which we refer to as the carboxysome-associated PII protein (CPII), represents a new and distinct subfamily within the broad superfamily of previously studied PII regulatory proteins, which are generally involved in regulating nitrogen metabolism in bacteria. CPII undergoes dramatic conformational changes in response to ADP binding, and the affinity for nucleotide binding is strongly enhanced by the presence of bicarbonate. CPII therefore appears to be a unique type of PII protein that senses bicarbonate availability, consistent with its apparent genomic association with the carboxysome and its constituents.
PubMed: 27464895
DOI: 10.1016/j.jmb.2016.07.015
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 5ds7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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