3TKK
Crystal Structure Analysis of a recombinant predicted acetamidase/ formamidase from the thermophile thermoanaerobacter tengcongensis
Replaces: 3MJJSummary for 3TKK
| Entry DOI | 10.2210/pdb3tkk/pdb |
| Descriptor | Predicted acetamidase/formamidase, CALCIUM ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | beta/alpha structure, hydrolase |
| Biological source | Thermoanaerobacter tengcongensis |
| Total number of polymer chains | 4 |
| Total formula weight | 129149.53 |
| Authors | |
| Primary citation | Qian, M.,Huang, Q.,Wu, G.,Lai, L.,Tang, Y.,Pei, J.,Kusunoki, M. Crystal Structure Analysis of a Recombinant Predicted Acetamidase/Formamidase from the Thermophile Thermoanaerobacter tengcongensis. PROTEIN J., 31:166-174, 2012 Cited by PubMed Abstract: The 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 P2₁, with unit-cell parameters a = 41.23 (3), b = 152.88 (6), c = 100.26 (7) Å, β = 99.49 (3) ° 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 Ca²⁺, 4 Zn²⁺ and 853 water molecules. The monomer is composed by the following: an N-domain which is featuring by three-layers β/β/β; a prominent excursion between N-terminal end of strand β₇ and β₁₁, which contains four-stranded antiparallel β sheet; an C-domain which is formed by the last 82 amino acid residues with the feature of mixed α/β structure. The protein contains ion-pair Ca²⁺-Zn²⁺. The portion of three-layer β/β/β along with the loops provides four protein ligands to the tightly bound Ca²⁺, three water molecules complete the coordination; and provides five protein ligands to the tightly bound Zn²⁺, one water molecule complete the coordination. PubMed: 22207484DOI: 10.1007/s10930-011-9387-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
Download full validation report
