Structural highlights
Publication Abstract from PubMedThe structure of acetamidase/formamidase (Amds/Fmds) from the archaeon Thermoanaerobacter tengcongensis has been determined by X-ray diffraction analysis using MAD data in a crystal of space group P2(1), with unit-cell parameters a = 41.23 (3), b = 152.88 (6), c = 100.26 (7) A, beta = 99.49 (3) degrees and been refined to a crystallographic R-factor of 17.4% and R-free of 23.7%. It contains two dimers in one asymmetric unit, in which native Amds/Fmds (TE19) contains of the 32 kDa native protein. The final model consists of 4 monomer (299 amino acids residues with additional 2 expression tag amino acids residues), 5 Ca(2+), 4 Zn(2+) and 853 water molecules. The monomer is composed by the following: an N-domain which is featuring by three-layers beta/beta/beta; a prominent excursion between N-terminal end of strand beta(7) and beta(11), which contains four-stranded antiparallel beta sheet; an C-domain which is formed by the last 82 amino acid residues with the feature of mixed alpha/beta structure. The protein contains ion-pair Ca(2+)-Zn(2+). The portion of three-layer beta/beta/beta along with the loops provides four protein ligands to the tightly bound Ca(2+), three water molecules complete the coordination; and provides five protein ligands to the tightly bound Zn(2+), one water molecule complete the coordination. Crystal Structure Analysis of a Recombinant Predicted Acetamidase/Formamidase from the Thermophile Thermoanaerobacter tengcongensis.,Qian M, Huang Q, Wu G, Lai L, Tang Y, Pei J, Kusunoki M Protein J. 2012 Feb;31(2):166-74. PMID:22207484[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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