SASDE96: Aldehyde dehydrogenase 12 from Zea mays Extrapolated to Infinite ...

Basic information

• Entry: Database: SASBDB / ID: SASDE96

Sample

Aldehyde dehydrogenase 12 from Zea mays Extrapolated to Infinite Dilution

• Aldehyde dehydrogenase 12 (protein), Zea mays

Function / homology

Function:

cellular response to chemical stimulus / L-glutamate gamma-semialdehyde dehydrogenase / 1-pyrroline-5-carboxylate dehydrogenase activity / aldehyde dehydrogenase (NAD+) activity

Domain/homology:

Aldehyde dehydrogenase family 7 member A1-like / Aldehyde dehydrogenase, cysteine active site / Aldehyde dehydrogenases cysteine active site. / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, N-terminal / Aldehyde dehydrogenase, C-terminal / Aldehyde/histidinol dehydrogenase

Component:

Aldehyde dehydrogenase 12

• Biological species: Zea mays (maize)
• Citation: Journal: J Mol Biol / Year: 2019; Title: Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.; Authors: David A Korasick / Radka Končitíková / Martina Kopečná / Eva Hájková / Armelle Vigouroux / Solange Moréra / Donald F Becker / Marek Šebela / John J Tanner / David Kopečný / ; Abstract: Heterokonts, Alveolata protists, green algae from Charophyta and Chlorophyta divisions, and all Embryophyta plants possess an aldehyde dehydrogenase (ALDH) gene named ALDH12. Here, we provide a biochemical characterization of two ALDH12 family members from the lower plant Physcomitrella patens and higher plant Zea mays. We show that ALDH12 encodes an NAD-dependent glutamate γ-semialdehyde dehydrogenase (GSALDH), which irreversibly converts glutamate γ-semialdehyde (GSAL), a mitochondrial intermediate of the proline and arginine catabolism, to glutamate. Sedimentation equilibrium and small-angle X-ray scattering analyses reveal that in solution both plant GSALDHs exist as equilibrium between a domain-swapped dimer and the dimer-of-dimers tetramer. Plant GSALDHs share very low-sequence identity with bacterial, fungal, and animal GSALDHs (classified as ALDH4), which are the closest related ALDH superfamily members. Nevertheless, the crystal structure of ZmALDH12 at 2.2-Å resolution shows that nearly all key residues involved in the recognition of GSAL are identical to those in ALDH4, indicating a close functional relationship with ALDH4. Phylogenetic analysis suggests that the transition from ALDH4 to ALDH12 occurred during the evolution of the endosymbiotic plant ancestor, prior to the evolution of green algae and land plants. Finally, ALDH12 expression in maize and moss is downregulated in response to salt and drought stresses, possibly to maintain proline levels. Taken together, these results provide molecular insight into the biological roles of the plant ALDH12 family.

Contact author

• David Korasick (Mizzou, University of Missouri-Columbia, Columbia, MO, USA)

Models

• Model #2495: ; Type: mix / Chi-square value: 0.577963245374368 / P-value: 0.000012; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2494: ; Type: mix / Chi-square value: 57.3783426075885; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Aldehyde dehydrogenase 12 from Zea mays Extrapolated to Infinite Dilution
• Buffer: Name: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM TCEP, and 5% (v/v) glycerol; pH: 7.8

Entity #1332

Type: protein / Description: Aldehyde dehydrogenase 12 / Formula weight: 60.397 / Num. of mol.: 4 / Source: Zea mays / References: UniProt: A0A2H4PMI3
Sequence:

MGSSHHHHHH SQDPAPFACV SRWLHTPSFA TVSPQEVSGS SPAEVQNFVQ GSWTASANWN WIVDPLNGDK FIKVAEVQGT EIKSFMESLS KCPKHGLHNP LKAPERYLMY GDISAKAAHM LGQPTVLDFF AKLIQRVSPK SYQQALAEVQ VSQKFLENFC GDQVRFLARS FAVPGNHLGQ RSNGYRWPYG PVAIITPFNF PLEIPLLQLM GALYMGNKPV LKVDSKVSIV MEQMIRLLHD CGLPAEDMDF INSDGAVMNK LLLEANPKMT LFTGSSRVAE KLAADLKGRV KLEDAGFDWK ILGPDVQEVD YVAWVCDQDA YACSGQKCSA QSVLFMHKNW SSSGLLEKMK KLSERRKLED LTIGPVLTVT TEAMIEHMNN LLKIRGSKVL FGGEPLANHS IPKIYGAMKP TAVFVPLEEI LKSGNFELVT KEIFGPFQVV TEYSEDQLEL VLEACERMNA HLTAAIVSND PLFLQDVLGR SVNGTTYAGI RARTTGAPQN HWFGPAGDPR GAGIGTPEAI KLVWSCHREI IYDVGPVPES WALPSAT

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 12 from Zea mays Extrapolated to Infinite Dilution
Measurement date: Dec 6, 2016 / Storage temperature: 4 °C / Cell temperature: 10 °C / Exposure time: 0.3 sec. / Number of frames: 33 / Unit: 1/A /

	Min	Max
Q	0.0131	0.5924

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 953 /

	Min	Max
Q	0.013683	0.592387
P(R) point	1	953
R	0	144.3

Result

Type of curve: extrapolated
Comments: This is the background subtracted experimental SAXS data extrapolated to infinite dilution. The original experiment consisted of static SAXS samples collected at 3 protein concentrations in the range of 0.9 - 2.6 mg/mL. The data were extrapolated to infinite dilution to account for sample aggregation in the two higher concentration samples. The corresponding model fits of the tetramer (top) and dimer (bottom) demonstrate that the dimer does not fit the SAXS data.

	Experimental	Porod
MW	249.8 kDa	219 kDa
Volume	-	351 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	90.51	92.63	0.5
Radius of gyration, Rg	4.02 nm	4.14 nm	0.03

	Min	Max
D	-	14.43
Guinier point	1	31