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Titolo:
Global folds of proteins with low densities of NOEs using residual dipolarcouplings: Application to the 370-residue maltodextrin-binding protein
Autore:
Mueller, GA; Choy, WY; Yang, DW; Forman-Kay, JD; Venters, RA; Kay, LE;
Indirizzi:
Univ Toronto, Prot Engn Network Ctr Excellence, Dept Med Genet, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 Genet, Toronto, ON M5S 1A8, Canada Univ Toronto, Prot Engn Network Ctr Excellence, Dept Microbiol Biochem & Chem, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 Chem, Toronto, ON M5S 1A8, Canada Hosp Sick Children, Toronto, ON M5G 1X8, Canada Hosp Sick Children Toronto ON Canada M5G 1X8 Toronto, ON M5G 1X8, Canada Duke Univ, Med Ctr, Durham, NC 27710 USA Duke Univ Durham NC USA 27710Duke Univ, Med Ctr, Durham, NC 27710 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 300, anno: 2000,
pagine: 197 - 212
SICI:
0022-2836(20000630)300:1<197:GFOPWL>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBONIC-ANHYDRASE-II; CHEMICAL-SHIFT; MALTOSE-BINDING; PERDEUTERATED PROTEINS; C-13-LABELED PROTEINS; MULTIDIMENSIONAL NMR; H-2-LABELED PROTEINS; BETA-CYCLODEXTRIN; ESCHERICHIA-COLI; ACTIVE-TRANSPORT;
Keywords:
dipolar couplings; protein structure; labeling; maltodextrin binding protein; protein domains;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Kay, LE Univ Toronto, Prot Engn Network Ctr Excellence, Dept Med Genet, 100 Coll St, Toronto, ON M5S 1A8, Canada Univ Toronto 100 Coll St Toronto ON Canada M5S 1A8 M5S 1A8, Canada
Citazione:
G.A. Mueller et al., "Global folds of proteins with low densities of NOEs using residual dipolarcouplings: Application to the 370-residue maltodextrin-binding protein", J MOL BIOL, 300(1), 2000, pp. 197-212

Abstract

The global fold of maltose-binding protein in complex with the substrate beta-cyclodextrin was determined by solution NMR methods. The two-domain protein is comprised of a single polypeptide chain of 370 residues, with a molecular mass of 42 kDa. Distance information in the form of H-N-H-N, H-N-CH3and CH3-CH3 NOEs was recorded on N-15, H-2 and N-15, C-13, H-2-labeled proteins with methyl protonation in Val, Leu, and Ile (C-delta 1 only) residues. Distances to methyl protons, critical for the Structure determination, comprised 77% of the long-range restraints. Initial structures were calculated on the basis of 1943 NOEs, 48 hydrogen bond and 555 dihedral angle restraints. A global pair-wise backbone rmsd of 5.5 Angstrom was obtained for these initial structures with rmsd values for the N and C domains of 2.4 and 3.8 Angstrom, respectively. Direct refinement against one-bond 1H(N)-N-15, C-13(alpha)-(CO)-C-13, N-15-(CO)-C-13, two-bond H-1(N)-(CO)-C-13 and three-bond H-1(N)-C-13(alpha) dipolar couplings resulted in structures with largenumbers of dipolar restraint violations. As an alternative to direct refinement against measured dipolar couplings we have developed an approach where discrete orientations are calculated for each peptide plane on the basis of the diyolar couplings described above. The orientation which best matches that in initial NMR structures calculated from NOE and dihedral angle restraints exclusively is used to refine further the structures using a new module written for CNS. Modeling studies from four different proteins with diverse structural motifs establishes the utility of the methodology. When applied to experimental data recorded on MBP the precision of the family of structures generated improves from 5.5 to 2.2 Angstrom, while the rmsd with respect to the X-ray structure (1dmb) is reduced from 5.1 to 3.3 Angstrom. (C) 2000 Academic Press.

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Documento generato il 05/07/20 alle ore 00:37:51