2Z10
Crystal structure of putative acetyltransferase
2Z10 の概要
| エントリーDOI | 10.2210/pdb2z10/pdb |
| 分子名称 | Ribosomal-protein-alanine acetyltransferase (2 entities in total) |
| 機能のキーワード | alpha/beta protein, acyltransferase, transferase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi |
| 由来する生物種 | Thermus thermophilus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 22288.47 |
| 構造登録者 | Murayama, K.,Kato-Murayama, M.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2007-05-07, 公開日: 2007-11-13, 最終更新日: 2024-11-20) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.77 Å) |
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