High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluste...
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International Union of Crystallography
2016-03-01
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| Series: | IUCrJ |
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| Online Access: | http://scripts.iucr.org/cgi-bin/paper?S2052252515024161 |
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| author | E. I. Howard B. Guillot M. P. Blakeley M. Haertlein M. Moulin A. Mitschler A. Cousido-Siah F. Fadel W. M. Valsecchi Takashi Tomizaki T. Petrova J. Claudot A. Podjarny |
| author_facet | E. I. Howard B. Guillot M. P. Blakeley M. Haertlein M. Moulin A. Mitschler A. Cousido-Siah F. Fadel W. M. Valsecchi Takashi Tomizaki T. Petrova J. Claudot A. Podjarny |
| author_sort | E. I. Howard |
| collection | DOAJ |
| description | Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluster of water molecules and the bound oleic acid in the H-FABP large internal cavity. The jointly refined X-ray/neutron structure of H-FABP was complemented by a transferred multipolar electron-density distribution using the parameters of the ELMAMII library. The resulting electron density allowed a precise determination of the electrostatic potential in the fatty acid (FA) binding pocket. Bader's quantum theory of atoms in molecules was then used to study interactions involving the internal water molecules, the FA and the protein. This approach showed H...H contacts of the FA with highly conserved hydrophobic residues known to play a role in the stabilization of long-chain FAs in the binding cavity. The determination of water hydrogen (deuterium) positions allowed the analysis of the orientation and electrostatic properties of the water molecules in the very ordered cluster. As a result, a significant alignment of the permanent dipoles of the water molecules with the protein electrostatic field was observed. This can be related to the dielectric properties of hydration layers around proteins, where the shielding of electrostatic interactions depends directly on the rotational degrees of freedom of the water molecules in the interface. |
| first_indexed | 2024-12-24T04:27:22Z |
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| id | doaj.art-bf03bda19f924cbeaba538d74a54fb78 |
| institution | Directory Open Access Journal |
| issn | 2052-2525 |
| language | English |
| last_indexed | 2024-12-24T04:27:22Z |
| publishDate | 2016-03-01 |
| publisher | International Union of Crystallography |
| record_format | Article |
| series | IUCrJ |
| spelling | doaj.art-bf03bda19f924cbeaba538d74a54fb782022-12-21T17:15:32ZengInternational Union of CrystallographyIUCrJ2052-25252016-03-013211512610.1107/S2052252515024161tj5008High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distributionE. I. Howard0B. Guillot1M. P. Blakeley2M. Haertlein3M. Moulin4A. Mitschler5A. Cousido-Siah6F. Fadel7W. M. Valsecchi8Takashi Tomizaki9T. Petrova10J. Claudot11A. Podjarny12Department of Integrative Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Centre de Biologie Intégrative, CNRS, INSERM, UdS, 1 rue Laurent Fries, 67404 Illkirch CEDEX, FranceCNRS and Université de Lorraine, Laboratoire CRM2, UMR 7036, Vandoeuvre-lès-Nancy, F-54506, FranceInstitut Laue–Langevin, 71 avenue des Martyrs, 38000 Grenoble, FranceILL–EMBL Deuteration Laboratory, Partnership for Structural Biology, 71 avenue des Martyrs, Grenoble 38000, FranceILL–EMBL Deuteration Laboratory, Partnership for Structural Biology, 71 avenue des Martyrs, Grenoble 38000, FranceDepartment of Integrative Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Centre de Biologie Intégrative, CNRS, INSERM, UdS, 1 rue Laurent Fries, 67404 Illkirch CEDEX, FranceDepartment of Integrative Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Centre de Biologie Intégrative, CNRS, INSERM, UdS, 1 rue Laurent Fries, 67404 Illkirch CEDEX, FranceDepartment of Integrative Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Centre de Biologie Intégrative, CNRS, INSERM, UdS, 1 rue Laurent Fries, 67404 Illkirch CEDEX, FranceInstituto de Química y Fisicoquímica Biológicas, Universidad de Buenos Aires, Junín 956, C1113AAD, Buenos Aires, ArgentinaSwiss Light Source, Paul Scherrer Institute, 5232 Villigen PSI, SwitzerlandInstitute of Mathematical Problems of Biology, Russian Academy of Sciences, Pushchino 142290, Russian FederationCNRS and Université de Lorraine, Laboratoire CRM2, UMR 7036, Vandoeuvre-lès-Nancy, F-54506, FranceDepartment of Integrative Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Centre de Biologie Intégrative, CNRS, INSERM, UdS, 1 rue Laurent Fries, 67404 Illkirch CEDEX, FranceCrystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluster of water molecules and the bound oleic acid in the H-FABP large internal cavity. The jointly refined X-ray/neutron structure of H-FABP was complemented by a transferred multipolar electron-density distribution using the parameters of the ELMAMII library. The resulting electron density allowed a precise determination of the electrostatic potential in the fatty acid (FA) binding pocket. Bader's quantum theory of atoms in molecules was then used to study interactions involving the internal water molecules, the FA and the protein. This approach showed H...H contacts of the FA with highly conserved hydrophobic residues known to play a role in the stabilization of long-chain FAs in the binding cavity. The determination of water hydrogen (deuterium) positions allowed the analysis of the orientation and electrostatic properties of the water molecules in the very ordered cluster. As a result, a significant alignment of the permanent dipoles of the water molecules with the protein electrostatic field was observed. This can be related to the dielectric properties of hydration layers around proteins, where the shielding of electrostatic interactions depends directly on the rotational degrees of freedom of the water molecules in the interface.http://scripts.iucr.org/cgi-bin/paper?S2052252515024161Neutron protein crystallographyhigh-resolution room-temperature X-ray crystallographyfatty acid binding proteinprotein hydration layerAIM topological properties |
| spellingShingle | E. I. Howard B. Guillot M. P. Blakeley M. Haertlein M. Moulin A. Mitschler A. Cousido-Siah F. Fadel W. M. Valsecchi Takashi Tomizaki T. Petrova J. Claudot A. Podjarny High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution IUCrJ Neutron protein crystallography high-resolution room-temperature X-ray crystallography fatty acid binding protein protein hydration layer AIM topological properties |
| title | High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution |
| title_full | High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution |
| title_fullStr | High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution |
| title_full_unstemmed | High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution |
| title_short | High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution |
| title_sort | high resolution neutron and x ray diffraction room temperature studies of an h fabp oleic acid complex study of the internal water cluster and ligand binding by a transferred multipolar electron density distribution |
| topic | Neutron protein crystallography high-resolution room-temperature X-ray crystallography fatty acid binding protein protein hydration layer AIM topological properties |
| url | http://scripts.iucr.org/cgi-bin/paper?S2052252515024161 |
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