EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer.
ジャーナル・号・ページ	J Mol Biol, Vol. 431, Issue 3, Page 524-541, Year 2019
掲載日	2019年2月1日
著者	Li-Kai Liu / John J Tanner /
PubMed 要旨	The aldehyde dehydrogenase (ALDH) superfamily is a vast group of enzymes that catalyze the NAD-dependent oxidation of aldehydes to carboxylic acids. ALDH16 is perhaps the most enigmatic member of the ...The aldehyde dehydrogenase (ALDH) superfamily is a vast group of enzymes that catalyze the NAD-dependent oxidation of aldehydes to carboxylic acids. ALDH16 is perhaps the most enigmatic member of the superfamily, owing to its extra C-terminal domain of unknown function and the absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences. Herein we report the first production of recombinant ALDH16, the first biochemical characterization of ALDH16, and the first crystal structure of ALDH16. Recombinant expression systems were generated for the bacterial ALDH16 from Loktanella sp. and human ALDH16A1. Four high-resolution crystal structures of Loktanella ALDH16 were determined. Loktanella ALDH16 is found to be a bona fide enzyme, exhibiting NAD-binding, ALDH activity, and esterase activity. In contrast, human ALDH16A1 apparently lacks measurable aldehyde oxidation activity, suggesting that it is a pseudoenzyme, consistent with the absence of the catalytic Cys in its sequence. The fold of ALDH16 comprises three domains: NAD-binding, catalytic, and C-terminal. The latter is unique to ALDH16 and features a Rossmann fold connected to a protruding β-flap. The tertiary structural interactions of the C-terminal domain mimic the quaternary structural interactions of the classic ALDH superfamily dimer, a phenomenon we call "trans-hierarchical structural similarity." ALDH16 forms a unique dimer in solution, which mimics the classic ALDH superfamily dimer-of-dimer tetramer. Small-angle X-ray scattering shows that human ALDH16A1 has the same dimeric structure and fold as Loktanella ALDH16. We suggest that the Loktanella ALDH16 structure may be considered to be the archetype of the ALDH16 family.
リンク	J Mol Biol / PubMed:30529746 / PubMed Central
手法	SAS (X-ray synchrotron) / X線回折
解像度	1.488 - 2.3 Å
構造データ	SASDE47: Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 2 mg/ml 手法: SAXS/SANS SASDE57: Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 4 mg/ml 手法: SAXS/SANS SASDE67: Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 6 mg/ml 手法: SAXS/SANS SASDE77: Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 8 mg/ml 手法: SAXS/SANS SASDE87: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1 mg/ml 手法: SAXS/SANS SASDE97: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1.6 mg/ml 手法: SAXS/SANS SASDEA7: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 3.2 mg/ml 手法: SAXS/SANS PDB-6mvr: Structure of a bacterial ALDH16 手法: X-RAY DIFFRACTION / 解像度: 1.95 Å PDB-6mvs: Structure of a bacterial ALDH16 complexed with NAD 手法: X-RAY DIFFRACTION / 解像度: 1.65 Å PDB-6mvt: Structure of a bacterial ALDH16 complexed with NADH 手法: X-RAY DIFFRACTION / 解像度: 2.3 Å PDB-6mvu: Structure of a bacterial ALDH16 active site mutant C295A complexed with p-nitrophenylacetate 手法: X-RAY DIFFRACTION / 解像度: 1.488 Å
化合物	ChemComp-SO4: SULFATE ION / 硫酸ジアニオン ChemComp-GOL: GLYCEROL / グリセロ-ル ChemComp-HOH: WATER ChemComp-NAD: NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NADYM ChemComp-NAI: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / NADH ChemComp-NA: Unknown entry / ナトリウムカチオン ChemComp-K4V*: 4-nitrophenyl acetate
由来	loktanella sp. 3andimar09 (バクテリア) Homo sapiens (ヒト)
キーワード	OXIDOREDUCTASE / ALDEHYDE DEHYDROGENASE / ALDH16 / NAD / ROSSMANN FOLD