3R5H

Crystal Structure of ADP-AIR complex of purK: N5-carboxyaminoimidazole ribonucleotide synthetase

3R5H の概要

• エントリーDOI: 10.2210/pdb3r5h/pdb
• 分子名称: Phosphoribosylaminoimidazole carboxylase, ATPase subunit, ADENOSINE-5'-DIPHOSPHATE, 5-AMINOIMIDAZOLE RIBONUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: carboxylase, lyase
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87912.09

構造登録者

Fung, L.W.,Tuntland, M.L.,Santarsiero, B.D.,Johnson, M.E. (登録日: 2011-03-18, 公開日: 2012-03-21, 最終更新日: 2023-11-01)

主引用文献

Tuntland, M.L.,Santarsiero, B.D.,Johnson, M.E.,Fung, L.W.
Elucidation of the bicarbonate binding site and insights into the carboxylation mechanism of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis
Acta Crystallogr.,Sect.D, 70:3057-3065, 2014

PubMed Abstract: Structures of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis with various combinations of ATP, ADP, Mg(2+), bicarbonate and aminoimidazole ribonucleotide (AIR) in the active site are presented. The binding site of bicarbonate has only been speculated upon previously, but is shown here for the first time. The binding involves interactions with the conserved residues Arg272, His274 and Lys348. These structures provide insights into each ligand in the active site and allow a possible mechanism to be proposed for the reaction that converts bicarbonate and AIR, in the presence of ATP, to produce (N(5))-carboxyaminoimidazole ribonucleotide. The formation of a carboxyphosphate intermediate through ATP phosphoryl transfer is proposed, followed by carboxylation of AIR to give the product, facilitated by a cluster of conserved residues and an active-site water network.

PubMed: 25372694
DOI: 10.1107/S1399004714021166

実験手法

X-RAY DIFFRACTION (2.2 Å)