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2EJX

Crystal structure of the hypothetical protein STK_08120 from Sulfolobus tokodaii

Summary for 2EJX
Entry DOI10.2210/pdb2ejx/pdb
DescriptorSTK_08120 (2 entities in total)
Functional Keywordsarcaea, stk_08120, structural genomics, unknown function, nppsfa, national project on protein structural and functional analyses
Biological sourceSulfolobus tokodaii str. 7
Total number of polymer chains1
Total formula weight16015.57
Authors
Miyakawa, T.,Miyazono, K.,Sawano, Y.,Hatano, K.,Nagata, K.,Tanokura, M. (deposition date: 2007-03-21, release date: 2008-03-25, Last modification date: 2024-03-13)
Primary citationMiyakawa, T.,Sawano, Y.,Miyazono, K.,Miyauchi, Y.,Hatano, K.,Tanokura, M.
A thermoacidophile-specific protein family, DUF3211, functions as a fatty acid carrier with novel binding mode
J.Bacteriol., 195:4005-4012, 2013
Cited by
PubMed Abstract: 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-Å resolution to predict its probable function using structure similarity searches. The structure adopts an α/β 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 affinity equal to that for 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 suggest that the thermoacidophile-specific protein family DUF3211 functions as a fatty acid carrier with a novel binding mode.
PubMed: 23836863
DOI: 10.1128/JB.00432-13
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.79 Å)
Structure validation

243911

数据于2025-10-29公开中

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