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Titolo:
AN INVESTIGATION OF THE LIGAND-BINDING SITE OF THE GLUTAMINE-BINDING PROTEIN OF ESCHERICHIA-COLI USING ROTATIONAL-ECHO DOUBLE-RESONANCE NMR
Autore:
HING AW; TJANDRA N; COTTAM PF; SCHAEFER J; HO C;
Indirizzi:
WASHINGTON UNIV,DEPT CHEM,1 BROOKINGS DR ST LOUIS MO 63130 WASHINGTON UNIV,DEPT CHEM ST LOUIS MO 63130 CARNEGIE MELLON UNIV,DEPT BIOL SCI PITTSBURGH PA 15213
Titolo Testata:
Biochemistry
fascicolo: 29, volume: 33, anno: 1994,
pagine: 8651 - 8661
SICI:
0006-2960(1994)33:29<8651:AIOTLS>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; SOLID-STATE NMR; DEPENDENT ACTIVE-TRANSPORT; RELAXATION MATRIX APPROACH; ISOLATED MEMBRANE-VESICLES; D-LACTATE DEHYDROGENASE; INTERATOMIC DISTANCE; TRYPTOPHAN RESIDUES; HELICAL PEPTIDE; HYDROGEN-BONDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
A.W. Hing et al., "AN INVESTIGATION OF THE LIGAND-BINDING SITE OF THE GLUTAMINE-BINDING PROTEIN OF ESCHERICHIA-COLI USING ROTATIONAL-ECHO DOUBLE-RESONANCE NMR", Biochemistry, 33(29), 1994, pp. 8651-8661

Abstract

Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance (REDOR) solid-state nuclear magnetic resonance (NMR) has beenused to determine internuclear distances in the complex of GlnBP and its ligand, L-glutamine. REDOR, combined with strategically placed isotopic labels, is effective in obtaining model-independent internucleardistances and thus detailed structural information on the ligand-binding site of GlnBP. The existence of a single histidine residue (His156) in the binding site has provided an excellent probe for distance measurements between protein and ligand. REDOR distances up to 6.3 Angstrom have been observed between C-13 labels in L-glutamine and N-15 labels in His156. These results have unambiguously determined the ligand orientation with respect to the imidazole ring of His156, which is an important first step in refining the ligand-binding-site model of GlnBPin general. The measured distances were also used as constraints in restrained molecular dynamics calculations of the complex using the unliganded crystal structure of GlnBP as the starting point. The simulations clearly show consistency between calculated distances and those measured by REDOR.

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Documento generato il 03/12/20 alle ore 15:49:11