Structural highlights
Publication Abstract from PubMed
STK_08120 is a member of the thermoacidophile-specific DUF3211 protein family from Sulfolobus tokodaii strain 7. Its molecular function remains obscure, and sequence similarities for obtaining functional remarks are not available. In this study, the crystal structure of STK_08120 was determined at 1.79 A resolution to predict its probable function using structure similarity searches. The structure adopts an alpha/beta structure of a helix-grip fold, which is found in the START domain proteins with cavities for hydrophobic substrates or ligands. The detailed structural features implied that fatty acids are the primary ligand candidates for STK_08120, and binding assays revealed that the protein bound long-chain saturated fatty acids (>C14) and their trans-unsaturated types with an equal affinity to major fatty acid binding proteins in mammals and plants. Moreover, the structure of an STK_08120-myristic acid complex revealed a unique binding mode among fatty acid binding proteins. These results propose that the thermoacidophile-specific protein family DUF3211 functions as a fatty acid carrier with novel binding mode.
A Thermoacidophile-Specific Protein Family, DUF3211, Functions as a Fatty Acid Carrier with Novel Binding Mode.,Miyakawa T, Sawano Y, Miyazono KI, Miyauchi Y, Hatano KI, Tanokura M J Bacteriol. 2013 Jul 8. PMID:23836863[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyakawa T, Sawano Y, Miyazono KI, Miyauchi Y, Hatano KI, Tanokura M. A Thermoacidophile-Specific Protein Family, DUF3211, Functions as a Fatty Acid Carrier with Novel Binding Mode. J Bacteriol. 2013 Jul 8. PMID:23836863 doi:10.1128/JB.00432-13
