Theoretical Study on the ATP Hydrolysis Mechanism of HisP Protein, the ATP-Binding Subunit of ABC Transporter

Autor:	Tetsuya Terasaki, Michihisa Koyama, Carlos A. Del Carpio, Ewa Broclawik, Akira Endou, Qiang Pei, Momoji Kubo, Akira Miyamoto, Kazumi Nishijima, Hideyuki Tsuboi
Rok vydání:	2007
Předmět:	Chemistry Permease Stereochemistry Mechanical Engineering Protein subunit Leaving group ATP-binding cassette transporter Condensed Matter Physics Hydrolysis Mechanics of Materials ATP hydrolysis General Materials Science Binding site Histidine
Zdroj:	MATERIALS TRANSACTIONS. 48:735-739
ISSN:	1347-5320 1345-9678
DOI:	10.2320/matertrans.48.735
Popis:	ATP binding subunit is known as a subunit of ABC transporter, providing energy through the binding of ATP with the subunit and the subsequent hydrolysis reaction of the bound ATP. In this study, density functional theory (DFT) method was used to study the ATP hydrolysis reaction in HisP protein, an ATP binding subunit of Histidine permease HisQMP2, by considering the ATP binding site, especially the � phosphate group, surrounding residues and water molecules. Based on DFT calculations, we proposed that ATP hydrolysis is initiated by the formation of Mg2þ mediated coordinate complex followed by the nucleophilic attack of a single water molecule (Water437) on the � -phosphate; the hydrolysis product ADP acts as a leaving group. The transition state structure was determined by an approximate saddle-point search. [doi:10.2320/matertrans.48.735]
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::edf0f7b5bedba90e98399a7de0c1bd49 https://doi.org/10.2320/matertrans.48.735 Zobrazit plný text záznamu