5D4P

Structure of CPII bound to ADP and bicarbonate, from Thiomonas intermedia K12

5D4P の概要

• エントリーDOI: 10.2210/pdb5d4p/pdb
• 関連するPDBエントリー: 5D4L 5D4M 5D4N 5D4O
• 分子名称: Putative Nitrogen regulatory protein P-II GlnB, ADENOSINE-5'-DIPHOSPHATE, BICARBONATE 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 binding, acetate binding, signaling protein
• 由来する生物種: Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 37561.31

構造登録者

Wheatley, N.M.,Ngo, J.,Cascio, D.,Sawaya, M.R.,Yeates, T.O. (登録日: 2015-08-08, 公開日: 2016-09-28, 最終更新日: 2023-09-27)

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

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

実験手法

X-RAY DIFFRACTION (2.2 Å)