1ifc: Difference between revisions
New page: left|200px<br /><applet load="1ifc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ifc, resolution 1.19Å" /> '''REFINEMENT OF THE ST... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ifc.jpg|left|200px]]<br /><applet load="1ifc" size=" | [[Image:1ifc.jpg|left|200px]]<br /><applet load="1ifc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ifc, resolution 1.19Å" /> | caption="1ifc, resolution 1.19Å" /> | ||
'''REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION'''<br /> | '''REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of the 131-residue rat intestinal fatty | The three-dimensional structure of the 131-residue rat intestinal fatty acid-binding protein, without bound ligand (apoI-FABP), has been refined with x-ray diffraction data to a nominal resolution of 1.19 A. The final model has a conventional crystallographic R-factor of 16.9% for 34,290 unique reflections [a root mean square (r.m.s.) deviation for bond length of 0.012 A and a r.m.s. deviation of 2.368 degrees for bond angles]. Ninety-two residues are present as components of the protein's 10 anti-parallel beta-strands while 14 residues are part of its two short alpha-helices. The beta-strands and alpha-helices are organized into two nearly orthogonal beta-sheets. Particular attention has been placed in defining solvent structure and the structures of discretely disordered groups in this protein. Two hundred thirty-seven solvent molecules have been identified; 24 are located within apoI-FABP. The refined model includes alternate conformers for 228 protein atoms (109 main-chain, 119 side-chain) and 63 solvent molecules. We have found several aromatic side-chains with multiple conformations located near, or in, the protein's ligand binding site. This observation, along with the fact that these side-chains have a temperature factor that is relatively higher than that of other aromatic residues, suggests that they may be involved in the process of noncovalent binding of fatty acid. The absence of a true hydrophobic core in I-FABP suggests that its structural integrity may be maintained primarily by a hydrogen bonding network involving protein and solvent atoms. | ||
==About this Structure== | ==About this Structure== | ||
1IFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | 1IFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFC OCA]. | ||
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gordon, J | [[Category: Gordon, J I.]] | ||
[[Category: Sacchettini, J | [[Category: Sacchettini, J C.]] | ||
[[Category: Scapin, G.]] | [[Category: Scapin, G.]] | ||
[[Category: lipid-binding protein]] | [[Category: lipid-binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:21 2008'' | ||
Revision as of 14:11, 21 February 2008
|
REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION
OverviewOverview
The three-dimensional structure of the 131-residue rat intestinal fatty acid-binding protein, without bound ligand (apoI-FABP), has been refined with x-ray diffraction data to a nominal resolution of 1.19 A. The final model has a conventional crystallographic R-factor of 16.9% for 34,290 unique reflections [a root mean square (r.m.s.) deviation for bond length of 0.012 A and a r.m.s. deviation of 2.368 degrees for bond angles]. Ninety-two residues are present as components of the protein's 10 anti-parallel beta-strands while 14 residues are part of its two short alpha-helices. The beta-strands and alpha-helices are organized into two nearly orthogonal beta-sheets. Particular attention has been placed in defining solvent structure and the structures of discretely disordered groups in this protein. Two hundred thirty-seven solvent molecules have been identified; 24 are located within apoI-FABP. The refined model includes alternate conformers for 228 protein atoms (109 main-chain, 119 side-chain) and 63 solvent molecules. We have found several aromatic side-chains with multiple conformations located near, or in, the protein's ligand binding site. This observation, along with the fact that these side-chains have a temperature factor that is relatively higher than that of other aromatic residues, suggests that they may be involved in the process of noncovalent binding of fatty acid. The absence of a true hydrophobic core in I-FABP suggests that its structural integrity may be maintained primarily by a hydrogen bonding network involving protein and solvent atoms.
About this StructureAbout this Structure
1IFC is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2-A resolution., Scapin G, Gordon JI, Sacchettini JC, J Biol Chem. 1992 Feb 25;267(6):4253-69. PMID:1740465
Page seeded by OCA on Thu Feb 21 13:11:21 2008