Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PHOSPHOHISTIDINES IN BACTERIAL SIGNALING
Autore:
MCEVOY MM; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOL BIOL EUGENE OR 97403
Titolo Testata:
Current opinion in structural biology
fascicolo: 6, volume: 7, anno: 1997,
pagine: 793 - 797
SICI:
0959-440X(1997)7:6<793:PIBS>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOCARRIER PROTEIN HPR; SUGAR PHOSPHOTRANSFERASE SYSTEM; RESTRAINED MOLECULAR-DYNAMICS; HISTIDINE-CONTAINING PROTEIN; CHEY-BINDING DOMAIN; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; CRYSTAL-STRUCTURE; IIA-DOMAIN; 3-DIMENSIONAL STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
M.M. Mcevoy e F.W. Dahlquist, "PHOSPHOHISTIDINES IN BACTERIAL SIGNALING", Current opinion in structural biology, 7(6), 1997, pp. 793-797

Abstract

The movement of Gram-negative bacteria in response to nutrients in the environment is driven by two interlinked chemotaxis systems, the methyl-accepting chemotaxis protein (MCP)-mediated pathway, and the phosphoenolpyruvate:sugar phosphotransferase (PTS)-mediated pathway. The physical link connecting the two systems is unclear, but the common utilization of histidine-containing phosphocarrier proteins is an intriguing similarity. The recent structure determinations of several proteinsfrom the PTS-mediated pathway, the phosphotransfer domain from the kinase CheA of the MCP-mediated chemotaxis pathway, and a homologous kinase, ArcB, enable the comparison of the histidine active sites of these systems. Overall, the tertiary folds of the proteins are quite different, as are the structural details of the histidine active sites within the proteins, and therefore there is not an obvious structural homolog via which the two pathways communicate, despite their similar chemical mechanisms. (C) Current Biology Ltd ISSN 0959-440X.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 04:38:09