SASDE57: Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 4 mg/ml

Basic information

• Entry: Database: SASBDB / ID: SASDE57

Sample

Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 4 mg/ml

• Aldehyde dehydrogenase 16 from Loktanella sp. (protein), LsALDH16, Loktanella sp. 3ANDIMAR09

• 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 / nucleotide binding / Aldehyde dehydrogenase
• Biological species: Loktanella sp. 3ANDIMAR09 (bacteria)
• 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 #2575: ; Type: atomic / Chi-square value: 0.773727266801379; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 4 mg/ml; Specimen concentration: 4 mg/ml
• Buffer: Name: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine; pH: 8

Entity #1354

Name: LsALDH16 / Type: protein / Description: Aldehyde dehydrogenase 16 from Loktanella sp. / Formula weight: 80.704 / Num. of mol.: 2 / Source: Loktanella sp. 3ANDIMAR09 / References: UniProt: A0A0Q3EUQ3
Sequence:

MTVKEIFETM DYGPAPESAK EAYAWLAEKG DFGHFIGGAW TAPGDLFATV NPATGQTLAQ VSQATQADVD AAVKAARKAQ PAWAKDGAAR ARVLYALARL LQKHARLFAV LETLDNGKPI REARDIDVPL AQRHFYHHAG YAQLMGTEMP DRAPLGVCGQ VIPWNFPLLM LAWKIAPALA MGNTVVLKPA EWTPLTALLF ADICGQAGVP AGVVNIVTGD GAVGEMIVTA QVDKVAFTGS TAVGRRIREA TAGTGKALSL ELGGKGPYVV CDDADIDSAV EGLVDAIWFN QGQVCCAGSR LLVQEGIADV FHAKLRARMD SLRIGDPLDK CIDIGAMVHP DQLARVRDMV AANTDGEVYQ TAVPAGCYYP PTLISGLAPA SPLMQQEIFG PVLVSTTFRT PAEAVEIANN TAYGLAASVW SENVNLALDL APKLVAGIVW INGTNMMDAA APFGGVRESG FGREGGWEGL AGYTRPAIAT KSPAAVAAYT GDGAADGLDR TAKLYIGGKQ TRPDGGYSRA VYGPKGKLLG HASLSNRKDL RNAVEAMNAA SGWSRTTGHL RAQILYFIGE NLSARADEFA NRIKDMTGKD GKAEVAASID RLFSAAAWAD KYDGQVKGVP LRGVALAMKE PVGKIGILCP DAAPLLGLVS LMAPAIAMGN RVTLAASEAF PLAATDFYQV LDTSDVPAGV VNILTGAHAD LAEPMARHLD LDAVWGLSGH AQVIEAASAG NLKRSWTGPF DPAHDHTRDI LSHATEVKTI WVPYGA

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 16 from Loktanella sp. (LsALDH16): 4 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	0.012	0.5642

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 549 /

	Min	Max
Q	0.01533	0.320768
P(R) point	1	549
R	0	112

Result

Type of curve: single_conc /

	Experimental	Porod
MW	151.3 kDa	-
Volume	-	204 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	742.2	746.46	1.11
Radius of gyration, Rg	3.57 nm	3.61 nm	0.04

	Min	Max
D	-	11.2
Guinier point	7	44