3ang | pdb_00003ang

Crystal structure of Thermus thermophilus FadR in complex with E. coli-derived dodecyl-CoA

spinqualitylabelsall models 3ang, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ang is a 4 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: DCC, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5SM42_THET8 Publication Abstract from PubMed In the extremely thermophilic bacterium Thermus thermophilus HB8, one of the four TetR family transcriptional regulators, which we named T. thermophilus FadR, negatively regulated the expression of several genes, including those involved in fatty acid degradation, both in vivo and in vitro. T. thermophilus FadR repressed the target gene expression by binding pseudopalindromic sequences covering the predicted -10 hexamers of their promoters, and medium to long straight-chain (C10-18) fatty acyl-CoA molecules were effective for transcriptional derepression. An X-ray crystal structure analysis revealed that T. thermophilus FadR bound one lauroyl (C12)-CoA molecule per FadR monomer, with its acyl chain moiety in the center of the FadR molecule, enclosed within a tunnel-like substrate-binding pocket surrounded by hydrophobic residues, and the CoA moiety interacting with basic residues on the protein surface. The growth of T. thermophilus HB8, with palmitic acid as the sole carbon source, increased the expression of FadR-regulated genes. These results indicate that in T. thermophilus HB8, medium to long straight-chain fatty acids can be used for metabolic energy under the control of FadR, although the major fatty acids found in this strain are iso- and anteiso-branched-chain (C15 and 17) fatty acids. TetR family transcriptional repressor Thermus thermophilus FadR controls fatty acid degradation.,Agari Y, Agari K, Sakamoto K, Kuramitsu S, Shinkai A Microbiology. 2011 Feb 24. PMID:21349973 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tetracycline repressor protein 3D structures

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