Data/hora: 23/06/2024 02:30:40

Biblioteca(s): 	Embrapa Agricultura Digital.	
Data corrente: 	16/12/2008	
Data da última atualização: 	15/01/2020	
Autoria: 	KUSER, P.; CUPRI, F.; BLEICHER, L.; POLIKARPOV, I.	
Afiliação: 	PAULA REGINA KUSER FALCAO, CNPTIA; FÁBIO CUPRI, Laboratório Nacional de Luz Síncrotron; LUCAS BLEICHER, USP; IGOR POLIKARPOV, USP.	
Título: 	Crystal structure of yeast hexokinase PI in complex with glucose: a classical "induced fit" example revised.	
Ano de publicação: 	2008	
Fonte/Imprenta: 	Proteins, v. 72, n. 2, p. 731-740, 2008.	
DOI: 	10.1002/prot.21956	
Idioma: 	Inglês	
Conteúdo: 	Hexokinase is the first enzyme in the glycolytic pathway that catalyzes the transfer of a phosphoryl group from ATP to glucose to form glucose-6-phosphate and ADP. Two yeast hexokinase isozymes are known, namely PI and PII. Here we redetermined the crystal structure of yeast hexokinase PI from Saccharomyces cerevisiae as a complex with its substrate, glucose, and refined it at 2.95 A resolution. Comparison of the holo-PI yeast hexokinase and apo-hexokinase structures shows in detail the rigid body domain closure and specific loop movements as glucose binds and sheds more light on structural basis of the "induced fit" mechanism of reaction in the HK enzymatic action. We also performed statistical coupling analysis of the hexokinase family, which reveals two co-evolved continuous clusters of amino acid residues and shows that the evolutionary coupled amino acid residues are mostly confined to the active site and the hinge region, further supporting the importance of these parts of the protein for the enzymatic catalysis.	
Palavras-Chave: 	Estrutura cristalina; Estrutura de raio-X de hexoquinase; Hexokinase X-ray structure; Statistical coupling analysis.	
Thesagro: 	Análise estatística; Glicose; Saccharomyces Cerevisiae.	
Categoria do assunto: 	--	
Registro original: 	Embrapa Agricultura Digital (CNPTIA)	
Exemplares: 	CNPTIA - (12445-1) - UPC - AP - -- -  -  - 2008.00204 - DES
CNPTIA - (12445-2) - UPC - AP - DD -  -  -  - DIS