Related ArticlesThe three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
J Biomol NMR. 1993 May;3(3):271-84
Authors: Andersen KV, Poulsen FM
The 3D structure of bovine recombinant acyl-coenzyme A binding protein has been determined using multidimensional heteronuclear magnetic resonance spectroscopy in a study that combines investigations of 15N-labeled and unlabeled protein. The present structure determination is a refinement of the structure previously determined (Andersen, K.V. and Poulsen, F.M. (1992) J. Mol. Biol., 226, 1131-1141). It is based on 1096 distance restraints and 124 dihedral angle restraints of which 69 are for phi-angles and 8 for chiral centers and 47 for prochiral centers. The new experimental input for the structure determination has provided an increase of 263 distance restraints, 5 phi-angle restraints, and 32 chi-angle restraints in 2 chiral centers, and 31 prochiral centers restraining an additional 23 chi 1, 8 chi 2, and 1 chi 3 angles. The increase of 300 distance and dihedral angle restraints representing an additional 30% of input parameters for the structure determination has been shown to be in agreement with the first structure. A set of 29 structures has been calculated and each of the structures has been compared to a mean structure to give an atomic root mean square deviation of 0.44 +/- 0.12 A (1 A is 0.1 nm) for the backbone atoms C, C alpha, and N in the four alpha-helices A1, residues 4-15, A2, residues 21-36, A3, residues 51-62 and A4, residues 65-84. The loop-region of residues Gly45-Lys50 could not be defined by the restraints obtained by NMR. The program PRONTO has been used for the spectrum analysis, assignment of the individual nuclear Overhauser effects, the integration of the cross peaks, and the measurement of the coupling constants. The programs DIANA, X-PLOR and INSIGHT have been used in the structure calculations and evaluations.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1137-40
Authors: Barnwal RP, Van Voorhis WC, Varani G
Abstract
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein...
nmrlearner
Journal club
0
09-10-2011 06:51 PM
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Aug;1808(8):2019-30
Authors: Romo TD, Bradney LA, Greathouse DV, Grossfield A
Abstract
One approach to the growing health problem of antibiotic resistant bacteria is the development of antimicrobial peptides (AMPs) as alternative treatments. The...
[NMR paper] Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C
Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Related Articles Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Biochemistry. 2001 Oct 23;40(42):12604-11
Authors: Beringhelli T, Goldoni L, Capaldi S, Bossi A, Perduca M, Monaco HL
Two different groups of liver fatty acid-binding proteins (L-FABPs) are known: the mammalian type and the basic type. Very few members of this second group of L-FABPs have been...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Bound water in apo and holo bovine heart fatty-acid-binding protein determined by het
Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy.
Related Articles Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy.
Eur J Biochem. 1998 Feb 1;251(3):781-6
Authors: Mesgarzadeh A, Pfeiffer S, Engelke J, Lassen D, Rüterjans H
Two- and three-dimensional heteronuclear NMR experiments have been performed to identify internally bound water molecules in the solution structure of bovine heart fatty-acid-binding protein...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
Biochemistry. 1997 Oct 21;36(42):12672-82
Authors: Poli-Scaife S, Attias R, Dansette PM, Mansuy D
Purified recombinant human liver cytochrome P450 2C9 was produced, from expression of the corresponding cDNA in yeast, in quantities large enough for UV-visible and 1H NMR experiments. Its...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] Three-dimensional structure of bovine heart fatty-acid-binding protein with bound pal
Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
Eur J Biochem. 1995 May 15;230(1):266-80
Authors: Lassen D, Lücke C, Kveder M, Mesgarzadeh A, Schmidt JM,...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] Three-dimensional structure of the FK506 binding protein/ascomycin complex in solutio
Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.
Related Articles Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.
Biochemistry. 1993 Jan 26;32(3):754-65
Authors: Meadows RP, Nettesheim DG, Xu RX, Olejniczak ET, Petros AM, Holzman TF, Severin J, Gubbins E, Smith H, Fesik SW
A high-resolution three-dimensional solution structure of the FKBP/ascomycin complex has been...
The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver:
Linear Mode
