Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Dissection of a (beta alpha)(8)-barrel enzyme into two folded halves
Autore:
Hocker, B; Beismann-Driemeyer, S; Hettwer, S; Lustig, A; Sterner, R;
Indirizzi:
Univ Gottingen, Inst Mikrobiol & Genet, Abt Mol Genet & Praparat Mol Biol,D-37077 Gottingen, Germany Univ Gottingen Gottingen Germany D-37077 Biol,D-37077 Gottingen, Germany Univ Cologne, Inst Biochem, D-50674 Cologne, Germany Univ Cologne Cologne Germany D-50674 t Biochem, D-50674 Cologne, Germany Univ Basel, Bioctr, Biophys Chem Abt, CH-4056 Basel, Switzerland Univ Basel Basel Switzerland CH-4056 hem Abt, CH-4056 Basel, Switzerland
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 1, volume: 8, anno: 2001,
pagine: 32 - 36
SICI:
1072-8368(200101)8:1<32:DOA(AE>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
HISTIDINE BIOSYNTHESIS; TRYPTOPHAN SYNTHASE; CIRCULAR-DICHROISM; ALPHA-SUBUNIT; PROTEIN; STABILITY; ISOMERASE; COMPLEMENTATION; BOUNDARIES; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Sterner, R Univ Gottingen, Inst Mikrobiol & Genet, Abt Mol Genet & Praparat Mol Biol,Grisebachstr 8, D-37077 Gottingen, Germany Univ Gottingen Grisebachstr 8 Gottingen Germany D-37077 ermany
Citazione:
B. Hocker et al., "Dissection of a (beta alpha)(8)-barrel enzyme into two folded halves", NAT ST BIOL, 8(1), 2001, pp. 32-36

Abstract

The (beta alpha)(8)-barrel, which is the most frequently encountered protein fold, is generally considered to consist of a single structural domain. However, the X-ray structure of the imidazoleglycerol phosphate synthase (HisF) from Thermotoga maritima has identified it as a (beta alpha)(8)-barrelmade up of two superimposable subdomains (HisF-N and HisF-C). HisF-N consists of the four N-terminal (beta alpha) units and HisF-C of the four C-terminal (beta alpha) units. It has been postulated, therefore, that HisF evolved by tandem duplication and fusion from an ancestral half-barrel. To test this hypothesis, HisF-N and HisF-C were produced in Escherichia coli, purified and characterized. Separately, HisF-N and HisF-C are folded proteins, but are catalytically inactive. Upon coexpression in vivo or joint refoldingin vitro, HisF-N and HisF-C assemble to the stoichiometric and catalytically fully active HisF-NC complex. These findings support the hypothesis thatthe (beta alpha)(8)-barrel of HisF evolved from an ancestral half-barrel and have implications for the folding mechanism of the members of this largeprotein family.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 23:06:54