1g74: Difference between revisions
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|PDB= 1g74 |SIZE=350|CAPTION= <scene name='initialview01'>1g74</scene>, resolution 1.7Å | |PDB= 1g74 |SIZE=350|CAPTION= <scene name='initialview01'>1g74</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ALBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= ALBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1g7n|1G7N]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g74 OCA], [http://www.ebi.ac.uk/pdbsum/1g74 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g74 RCSB]</span> | |||
}} | }} | ||
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[[Category: Banaszak, L J.]] | [[Category: Banaszak, L J.]] | ||
[[Category: Reese, A J.]] | [[Category: Reese, A J.]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: fatty acid binding]] | [[Category: fatty acid binding]] | ||
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[[Category: protein engineering]] | [[Category: protein engineering]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:59 2008'' | ||
Revision as of 20:37, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ALBP (Mus musculus) | ||||||
| Related: | 1G7N
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid bound form
OverviewOverview
The family of proteins accountable for the intracellular movement of lipids is characterized by a 10-stranded beta-barrel that forms an internalized cavity varying in size and binding preferences. The loop connecting beta-strands E and F (the fifth and sixth strands) is the most striking conformational difference between adipocyte lipid binding protein (ALBP; fatty acids) and cellular retinoic acid binding protein type I (CRABP I). A three-residue mutation was made in wild-type (WT)-ALBP [ALBP with a three-residue mutation (EF-ALBP)] to mimic CRABP I. Crystal structures of ligand-free and EF-ALBP with bound oleic acid were solved to resolutions of 1.5 A and 1.7 A, respectively, and compared with previous studies of WT-ALBP. The changes in three residues of one loop of the protein appear to have altered the positioning of the C18 fatty acid, as observed in the electron density of EF-ALBP. The crystallographic studies made it possible to compare the protein conformation and ligand positioning with those found in the WT protein. Although the cavity binding sites in both the retinoid and fatty acid binding proteins are irregular, the ligand atoms appear to favor a relatively planar region of the cavities. Preliminary chemical characterization of the mutant protein indicated changes in some binding properties and overall protein stability.
About this StructureAbout this Structure
1G74 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Specificity determinants for lipids bound to beta-barrel proteins., Reese AJ, Banaszak LJ, J Lipid Res. 2004 Feb;45(2):232-43. Epub 2003 Nov 1. PMID:14594993
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