SASDE87: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsA...

Basic information

• Entry: Database: SASBDB / ID: SASDE87

Sample

Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1 mg/ml

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

• Function / homology: Aldehyde dehydrogenase / oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, C-terminal / Aldehyde dehydrogenase, N-terminal / Aldehyde/histidinol dehydrogenase / membrane / Aldehyde dehydrogenase family 16 member A1
• Biological species: Homo sapiens (human)
• Citation: Journal: J Mol Biol / Year: 2019; Title: Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer.; Authors: Li-Kai Liu / John J Tanner / ; Abstract: 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.

Contact author

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

Models

• Model #2580: ; Type: atomic / Chi-square value: 1.09935715734597; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1 mg/ml; Specimen concentration: 1 mg/ml
• Buffer: Name: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine; pH: 8

Entity #1356

Name: HsALDH16A1 / Type: protein
Description: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens
Formula weight: 85.408 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q8IZ83
Sequence:

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

Experimental information

• Beam: Instrument name: Advanced Light Source (ALS) 12.3.1 (SIBYLS); City: Berkeley, CA / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.127 Å / Dist. spec. to detc.: 1.5 mm
• Detector: Name: Pilatus3 X 2M / Pixsize x: 172 mm

Scan

Title: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1 mg/ml
Measurement date: Dec 13, 2017 / Cell temperature: 10 °C / Exposure time: 0.3 sec. / Number of frames: 32 / Unit: 1/A /

	Min	Max
Q	0.0131	0.5642

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 550 /

	Min	Max
Q	0.015887	0.321883
P(R) point	1	550
R	0	109

Result

Type of curve: single_conc /

	Experimental	Porod
MW	147.1 kDa	-
Volume	-	230 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	131.9	130.99	0.61
Radius of gyration, Rg	3.67 nm	3.63 nm	1

	Min	Max
D	-	10.9
Guinier point	6	41