Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CRYSTAL-STRUCTURES OF CHEY FROM THERMOTOGA-MARITIMA DO NOT SUPPORT CONVENTIONAL EXPLANATIONS FOR THE STRUCTURAL BASIS OF ENHANCED THERMOSTABILITY
Autore:
USHER KC; DELACRUZ AFA; DAHLQUIST FW; SWANSON RV; SIMON MI; REMINGTON SJ;
Indirizzi:
UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV OREGON,DEPT CHEM EUGENE OR 97403 UNIV OREGON,DEPT PHYS EUGENE OR 97403 CALTECH,DEPT BIOL PASADENA CA 91125
Titolo Testata:
Protein science
fascicolo: 2, volume: 7, anno: 1998,
pagine: 403 - 412
SICI:
0961-8368(1998)7:2<403:COCFTD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARCHAEBACTERIUM PYROCOCCUS-FURIOSUS; ESCHERICHIA-COLI CHEY; BACTERIAL CHEMOTAXIS; SECONDARY STRUCTURE; MAGNESIUM BINDING; PROTEIN CHEY; RESOLUTION; STABILITY; SURFACE; NMR;
Keywords:
CHEMOTAXIS; PROTEIN CRYSTALLOGRAPHY; SIGNAL TRANSDUCTION; THERMOSTABILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
K.C. Usher et al., "CRYSTAL-STRUCTURES OF CHEY FROM THERMOTOGA-MARITIMA DO NOT SUPPORT CONVENTIONAL EXPLANATIONS FOR THE STRUCTURAL BASIS OF ENHANCED THERMOSTABILITY", Protein science, 7(2), 1998, pp. 403-412

Abstract

The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at upto 1.9 Angstrom resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the ''gamma-turn loop,'' residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 12:32:44