SASDE97: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsA...

基本情報

• 登録情報: データベース: SASBDB / ID: SASDE97

試料

Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1.6 mg/ml

• Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (protein), HsALDH16A1, Homo sapiens

• 機能・相同性: アルデヒドデヒドロゲナーゼ / oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, N-terminal / Aldehyde dehydrogenase, C-terminal / Aldehyde/histidinol dehydrogenase / 生体膜 / Aldehyde dehydrogenase family 16 member A1
• 生物種: Homo sapiens (ヒト)
• 引用: ジャーナル: J Mol Biol / 年: 2019; タイトル: Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer.; 著者: Li-Kai Liu / John J Tanner / ; 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 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.

登録者

• Li-Kai Liu (Mizzou, University of Missouri-Columbia, Columbia, MO, USA)

モデル

• モデル #2581: ; タイプ: atomic / カイ2乗値: 1.71067561262325; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1.6 mg/ml; 試料濃度: 1.6 mg/ml
• バッファ: 名称: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine; pH: 8

要素 #1356

名称: HsALDH16A1 / タイプ: protein
記述: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens
分子量: 85.408 / 分子数: 2 / 由来: Homo sapiens / 参照: UniProt: Q8IZ83
配列:

GSHMAATRAG PRAREIFTSL EYGPVPESHA CALAWLDTQD RCLGHYVNGK WLKPEHRNSV PCQDPITGEN LASCLQAQAE DVAAAVEAAR MAFKGWSAHP GVVRAQHLTR LAEVIQKHQR LLWTLESLVT GRAVREVRDG DVQLAQQLLH YHAIQASTQE EALAGWEPMG VIGLILPPTF SFLEMMWRIC PALAVGCTVV ALVPPASPAP LLLAQLAGEL GPFPGILNVL SGPASLVPIL ASQPGIRKVA FCGAPEEGRA LRRSLAGECA ELGLALGTES LLLLTDTADV DSAVEGVVDA AWSDRGPGGL RLLIQESVWD EAMRRLQERM GRLRSGRGLD GAVDMGARGA AACDLVQRFV REAQSQGAQV FQAGDVPSER PFYPPTLVSN LPPASPCAQV EVPWPVVVAS PFRTAKEALL VANGTPRGGS ASVWSERLGQ ALELGYGLQV GTVWINAHGL RDPSVPTGGC KESGCSWHGG PDGLYEYLRP SGTPARLSCL SKNLNYDTFG LAVPSTLPAG PEIGPSPAPP YGLFVGGRFQ APGARSSRPI RDSSGNLHGY VAEGGAKDIR GAVEAAHQAF PGWAGQSPGA RAALLWALAA ALERRKSTLA SRLERQGAEL KAAEAEVELS ARRLRAWGAR VQAQGHTLQV AGLRGPVLRL REPLGVLAVV CPDEWPLLAF VSLLAPALAY GNTVVMVPSA ACPLLALEVC QDMATVFPAG LANVVTGDRD HLTRCLALHQ DVQAMWYFGS AQGSQFVEWA SAGNLKPVWA SRGCPRAWDQ EAEGAGPELG LRVARTKALW LPMGD

実験情報

• ビーム: 設備名称: Advanced Light Source (ALS) 12.3.1 (SIBYLS) / 地域: Berkeley, CA / 国: USA / 線源: X-ray synchrotronシンクロトロン / 波長: 0.127 Å / スペクトロメータ・検出器間距離: 1.5 mm
• 検出器: 名称: Pilatus3 X 2M / Pixsize x: 172 mm

スキャン

タイトル: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1.6 mg/ml
測定日: 2017年12月13日 / セル温度: 10 °C / 照射時間: 0.3 sec. / フレーム数: 32 / 単位: 1/A /

	Min	Max
Q	0.012	0.5642

距離分布関数 P(R)

ソフトウェア P(R): GNOM 5.0 / ポイント数: 555 /

	Min	Max
Q	0.0131	0.321883
P(R) point	1	555
R	0	112

結果

カーブのタイプ: single_conc /

	実験値	Porod
分子量	156 kDa	-
体積	-	236 nm3

	P(R)	Guinier	Guinier error
前方散乱 I0	272.6	271.93	1
慣性半径, Rg	3.75 nm	3.75 nm	0.09

	Min	Max
D	-	11.2
Guinier point	1	41