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1bwy
From Proteopedia
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[[Image:1bwy.jpg|left|200px]] | [[Image:1bwy.jpg|left|200px]] | ||
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'''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN''' | '''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN''' | ||
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[[Category: Specht, B.]] | [[Category: Specht, B.]] | ||
[[Category: Spener, F.]] | [[Category: Spener, F.]] | ||
| - | [[Category: | + | [[Category: Fatty acid binding]] |
| - | [[Category: | + | [[Category: Fatty acid binding protein]] |
| - | [[Category: | + | [[Category: Heart muscle]] |
| - | [[Category: | + | [[Category: Intracellular lipid binding protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:03:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:03, 2 May 2008
NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN
Overview
The three-dimensional structure of the holo form of recombinant cellular bovine heart fatty-acid-binding protein (H-FABPc), a polypeptide of 133 amino acid residues with a molecular mass of 15 kDa, has been determined by multidimensional homonuclear and heteronuclear NMR spectroscopy applied to uniformly 15N-labeled and unlabeled protein. A nearly complete set of 1H and 15N chemical shift assignments was obtained. A total of 2329 intramolecular distance constraints and 42 side-chain chi 1 dihedral-angle constraints were derived from cross-relaxation and J coupling information. 3D nuclear Overhauser enhancement and exchange spectroscopy combined with heteronuclear multiple-quantum coherence (NOESY-HMQC) experiments, performed on a sample of uniformly 13C-labeled palmitic acid bound to unlabeled cellular heart fatty-acid-binding protein revealed 10 intermolecular contacts that determine the orientation of the bound fatty acid. An ensemble of protein conformations was calculated with the distance-geometry algorithm for NMR applications (DIANA) using the redundant dihedral-angle constraint (REDAC) strategy. After docking the fatty acid into the protein, the protein-ligand arrangement was subject to distance-restrained energy minimization. The overall conformation of the protein is a beta-barrel consisting of 10 antiparallel beta-strands which form two nearly orthogonal beta-sheets of five strands each. Two short helices form a helix-turn-helix motif in the N-terminal region of the polypeptide chain. The palmitic acid is bound within the protein in a U-shaped conformation close to the two helices. The obtained solution structure of the protein is consistent with a number of fatty-acid-binding-protein crystal structures.
About this Structure
1BWY is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy., Lassen D, Lucke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B, Lezius A, Spener F, Ruterjans H, Eur J Biochem. 1995 May 15;230(1):266-80. PMID:7601110 Page seeded by OCA on Fri May 2 12:03:29 2008
