2ZQ8
Apo structure of class a beta-lactamase Toho-1 R274N/R276N double mutant
2ZQ8 の概要
| エントリーDOI | 10.2210/pdb2zq8/pdb |
| 関連するPDBエントリー | 2ZQ7 2ZQ9 2ZQA 2ZQC 2ZQD |
| 分子名称 | Beta-lactamase Toho-1, SULFATE ION (3 entities in total) |
| 機能のキーワード | extended-spectrum, esbl, beta-lactamase, toho-1, hydrolase, antibiotic resistance, plasmid |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 28656.10 |
| 構造登録者 | Shimamura, T.,Nitanai, Y.,Uchiyama, T.,Ago, H.,Matsuzawa, H.,Miyano, M. (登録日: 2008-08-07, 公開日: 2009-07-28, 最終更新日: 2023-11-01) |
| 主引用文献 | Shimamura, T.,Nitanai, Y.,Uchiyama, T.,Matsuzawa, H. Improvement of crystal quality by surface mutations of beta-lactamase Toho-1 Acta Crystallogr.,Sect.F, 65:379-382, 2009 Cited by PubMed Abstract: The beta-lactamase Toho-1 exhibits a strong tendency to form merohedrally twinned crystals. Here, the crystal quality of Toho-1 was improved by using surface modification to remove a sulfate ion involved in crystal packing. The surface-modified Toho-1 variant (R274N/R276N) was crystallized under similar conditions to those used for wild-type Toho-1. R274N/R276N did not form merohedrally twinned crystals. The crystals diffracted to a significantly higher resolution (approximately 0.97 A) than the wild-type crystals (1.65 A); they belonged to the same space group and had almost identical unit-cell parameters to those of wild-type Toho-1. PubMed: 19342785DOI: 10.1107/S1744309109008240 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.03 Å) |
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