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Titolo:
A F-19-NMR STUDY OF THE MEMBRANE-BINDING REGION OF D-LACTATE DEHYDROGENASE OF ESCHERICHIA-COLI
Autore:
SUN ZY; TRUONG HTN; PRATT EA; SUTHERLAND DC; KULIG CE; HOMER RJ; GROETSCH SM; HSUE PY; HO C;
Indirizzi:
CARNEGIE MELLON UNIV,DEPT BIOL SCI PITTSBURGH PA 15213 CARNEGIE MELLON UNIV,DEPT BIOL SCI PITTSBURGH PA 15213
Titolo Testata:
Protein science
fascicolo: 11, volume: 2, anno: 1993,
pagine: 1938 - 1947
SICI:
0961-8368(1993)2:11<1938:AFSOTM>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; ACTIVE-TRANSPORT; VESICLES; PURIFICATION; RECONSTITUTION; SUBSTITUTIONS; MECHANISMS; SITE;
Keywords:
D-LACTATE DEHYDROGENASE; FLUOROPHENYLALANINES; 5-FLUOROTRYPTOPHAN; FLUOROTYROSINE; F-19-NMR; MEMBRANE-ASSOCIATED PROTEINS; NMR; SITE-SPECIFIC MUTAGENESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
Z.Y. Sun et al., "A F-19-NMR STUDY OF THE MEMBRANE-BINDING REGION OF D-LACTATE DEHYDROGENASE OF ESCHERICHIA-COLI", Protein science, 2(11), 1993, pp. 1938-1947

Abstract

D-Lactate dehydrogenase (D-LDH) is a membrane-associated respiratory enzyme of Escherichia coli. The protein is composed of 571 amino acid residues with a flavin adenine dinucleotide (FAD) cofactor, has a molecular weight of approximately 65,000, and requires lipids or detergents for full activity. We used NMR spectroscopy to investigate the structure Of D-LDH and its interaction with phospholipids. We incorporated 5-fluorotryptophan (5F-Trp) into the native enzyme, which contains five tryptophan residues, and into mutant enzymes, where a sixth tryptophan is substituted into a specific site by oligonucleotide-directed mutagenesis, and studied the 5F-Trp-labeled enzymes using F-19-NMR spectroscopy. In this way, information was obtained about the local environment at each native and substituted tryptophan site. Using a nitroxide spin-labeled fatty acid, which broadens the resonance from any residuewithin 15 angstrom, we have established that the membrane-binding area of the protein includes the region between Tyr 228 and Phe 369, but is not continuous within this region. This conclusion is strengthened by the results of F-19-NMR spectroscopy of wild-type enzyme labeled with fluorotyrosine or fluorophenylalanine in the presence and absence of a nitroxide spin-labeled fatty acid. These experiments indicate that9-10 Phe and 34 Tyr residues are located near the lipid phase.

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Documento generato il 03/12/20 alle ore 15:02:30