3VG7

Structure of human LFABP at high resolution from S-SAD

Summary for 3VG7

• Entry DOI: 10.2210/pdb3vg7/pdb
• Related: 3B2H 3B2I 3B2J 3B2K 3B2L 3VG2 3VG3 3VG4 3VG5 3VG6
• Descriptor: Fatty acid-binding protein, liver, PALMITIC ACID (3 entities in total)
• Functional Keywords: lfabp, s-sad, copper kalpha, palmitic acid, lipid binding protein
• Biological source: Homo Sapiens
• Cellular location: Cytoplasm: P07148
• Total number of polymer chains: 1
• Total formula weight: 15112.58

Authors

Sharma, A.,Yogavel, M.,Sharma, A. (deposition date: 2011-08-03, release date: 2012-08-01, Last modification date: 2024-03-20)

Primary citation

Sharma, A.,Yogavel, M.,Sharma, A.
Utility of anion and cation combinations for phasing of protein structures.
J.Struct.Funct.Genom., 13:135-143, 2012

PubMed Abstract: We report the use of anionic (I(-)), cationic (Ba(2+), Cd(2+)) and ionic mixtures (I(-) plus Ba(2+)) for derivatizing liver fatty acid binding protein (LFABP) crystals. Use of cationic and anionic salts in phasing experiments revealed distinct non-overlapping sites for these ions, suggesting exclusive binding regions on LFABP. Interestingly, cations of identical charge and valency (like Ba(2+) and Cd(2+)) bound to distinct pockets on the protein surface. Furthermore, a mixture of salts containing both I(-) and Ba(2+) was very useful in phasing experiments as these oppositely charged ions bound to different regions of LFABP. Our data therefore suggest that cationic and anionic salt mixtures like BaCl(2) with NH(4)I or salts like CdI, BaI where each ion has a significant anomalous signal for a given X-ray wavelength may be valuable reagents for phasing during structure determination.

PubMed: 22562242
DOI: 10.1007/s10969-012-9137-3

Experimental method

X-RAY DIFFRACTION (1.44 Å)