2Z0Z
Crystal structure of putative acetyltransferase
Summary for 2Z0Z
| Entry DOI | 10.2210/pdb2z0z/pdb |
| Descriptor | Putative uncharacterized protein TTHA1799, SULFATE ION (3 entities in total) |
| Functional Keywords | alpha/beta protein, transferase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 22738.95 |
| Authors | Murayama, K.,Kato-Murayama, M.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-05-07, release date: 2007-11-13, Last modification date: 2023-11-01) |
| Primary citation | Sakamoto, K.,Murayama, K.,Oki, K.,Iraha, F.,Kato-Murayama, M.,Takahashi, M.,Ohtake, K.,Kobayashi, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S. Genetic Encoding of 3-Iodo-l-Tyrosine in Escherichia coli for Single-Wavelength Anomalous Dispersion Phasing in Protein Crystallography Structure, 17:335-344, 2009 Cited by PubMed Abstract: We developed an Escherichia coli cell-based system to generate proteins containing 3-iodo-L-tyrosine at desired sites, and we used this system for structure determination by single-wavelength anomalous dispersion (SAD) phasing with the strong iodine signal. Tyrosyl-tRNA synthetase from Methanocaldococcus jannaschii was engineered to specifically recognize 3-iodo-L-tyrosine. The 1.7 A crystal structure of the engineered variant, iodoTyrRS-mj, bound with 3-iodo-L-tyrosine revealed the structural basis underlying the strict specificity for this nonnatural substrate; the iodine moiety makes van der Waals contacts with 5 residues at the binding pocket. E. coli cells expressing iodoTyrRS-mj and the suppressor tRNA were used to incorporate 3-iodo-L-tyrosine site specifically into the ribosomal protein N-acetyltransferase from Thermus thermophilus. The crystal structure of this enzyme with iodotyrosine was determined at 1.8 and 2.2 Angstroms resolutions by SAD phasing at CuK alpha and CrK alpha wavelengths, respectively. The native structure, determined by molecular replacement, revealed no significant structural distortion caused by iodotyrosine incorporation. PubMed: 19278648DOI: 10.1016/j.str.2009.01.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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