1bwy: Difference between revisions
New page: left|200px<br /><applet load="1bwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bwy" /> '''NMR STUDY OF BOVINE HEART FATTY ACID BINDING... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1bwy.jpg|left|200px]]<br /><applet load="1bwy" size=" | [[Image:1bwy.jpg|left|200px]]<br /><applet load="1bwy" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1bwy" /> | caption="1bwy" /> | ||
'''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN'''<br /> | '''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of the holo form of recombinant cellular | 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== | ==About this Structure== | ||
1BWY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | 1BWY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWY OCA]. | ||
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: Mesgarzadeh, A.]] | [[Category: Mesgarzadeh, A.]] | ||
[[Category: Rueterjans, H.]] | [[Category: Rueterjans, H.]] | ||
[[Category: Schmidt, J | [[Category: Schmidt, J M.]] | ||
[[Category: Specht, B.]] | [[Category: Specht, B.]] | ||
[[Category: Spener, F.]] | [[Category: Spener, F.]] | ||
| Line 27: | Line 27: | ||
[[Category: intracellular lipid binding protein]] | [[Category: intracellular lipid binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:08 2008'' | ||
Revision as of 13:00, 21 February 2008
|
NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN
OverviewOverview
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 StructureAbout this Structure
1BWY is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Feb 21 12:00:08 2008