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3WS5

N288Q-N321Q mutant BETA-LACTAMASE DERIVED FROM CHROMOHALOBACTER SP.560 (Condition-2B)

3WS5 の概要
エントリーDOI10.2210/pdb3ws5/pdb
関連するPDBエントリー3WRT 3WRZ 3WS0 3WS1 3WS2 3WS4
分子名称Beta-lactamase, STRONTIUM ION, CHLORIDE ION, ... (5 entities in total)
機能のキーワードcephalosporinase, hydrolase
由来する生物種Chromohalobacter sp. 560
タンパク質・核酸の鎖数3
化学式量合計119022.35
構造登録者
主引用文献Arai, S.,Yonezawa, Y.,Okazaki, N.,Matsumoto, F.,Shibazaki, C.,Shimizu, R.,Yamada, M.,Adachi, M.,Tamada, T.,Kawamoto, M.,Tokunaga, H.,Ishibashi, M.,Blaber, M.,Tokunaga, M.,Kuroki, R.
Structure of a highly acidic beta-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site
Acta Crystallogr.,Sect.D, 71:541-554, 2015
Cited by
PubMed Abstract: Environmentally friendly absorbents are needed for Sr(2+) and Cs(+), as the removal of the radioactive Sr(2+) and Cs(+) that has leaked from the Fukushima Nuclear Power Plant is one of the most important problems in Japan. Halophilic proteins are known to have many acidic residues on their surface that can provide specific binding sites for metal ions such as Cs(+) or Sr(2+). The crystal structure of a halophilic β-lactamase from Chromohalobacter sp. 560 (HaBLA) was determined to resolutions of between 1.8 and 2.9 Å in space group P31 using X-ray crystallography. Moreover, the locations of bound Sr(2+) and Cs(+) ions were identified by anomalous X-ray diffraction. The location of one Cs(+)-specific binding site was identified in HaBLA even in the presence of a ninefold molar excess of Na(+) (90 mM Na(+)/10 mM Cs(+)). From an activity assay using isothermal titration calorimetry, the bound Sr(2+) and Cs(+) ions do not significantly affect the enzymatic function of HaBLA. The observation of a selective and high-affinity Cs(+)-binding site provides important information that is useful for the design of artificial Cs(+)-binding sites that may be useful in the bioremediation of radioactive isotopes.
PubMed: 25760604
DOI: 10.1107/S1399004714027734
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 3ws5
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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