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

基本情報

• 登録情報: データベース: SASBDB / ID: SASDE96

試料

Aldehyde dehydrogenase 12 from Zea mays Extrapolated to Infinite Dilution

• Aldehyde dehydrogenase 12 (protein), Zea mays

機能・相同性

分子機能:

L-glutamate gamma-semialdehyde dehydrogenase / L-glutamate gamma-semialdehyde dehydrogenase activity / aldehyde dehydrogenase (NAD+) activity / nucleotide binding

ドメイン・相同性:

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, C-terminal / Aldehyde dehydrogenase, N-terminal / Aldehyde/histidinol dehydrogenase

構成要素:

Aldehyde dehydrogenase 12

• 生物種: Zea mays (トウモロコシ)
• 引用: ジャーナル: J Mol Biol / 年: 2019; タイトル: Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.; 著者: David A Korasick / Radka Končitíková / Martina Kopečná / Eva Hájková / Armelle Vigouroux / Solange Moréra / Donald F Becker / Marek Šebela / John J Tanner / David Kopečný / ; 要旨: 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.

登録者

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

モデル

• モデル #2495: ; タイプ: mix / カイ2乗値: 0.577963245374368 / P-value: 0.000012; Omokage検索でこの集合体の類似形状データを探す (詳細)
• モデル #2494: ; タイプ: mix / カイ2乗値: 57.3783426075885; 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 12 from Zea mays Extrapolated to Infinite Dilution
• バッファ: 名称: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM TCEP, and 5% (v/v) glycerol; pH: 7.8

要素 #1332

タイプ: protein / 記述: Aldehyde dehydrogenase 12 / 分子量: 60.397 / 分子数: 4 / 由来: Zea mays / 参照: UniProt: A0A2H4PMI3
配列:

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

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 / 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 12 from Zea mays Extrapolated to Infinite Dilution
測定日: 2016年12月6日 / 保管温度: 4 °C / セル温度: 10 °C / 照射時間: 0.3 sec. / フレーム数: 33 / 単位: 1/A /

	Min	Max
Q	0.0131	0.5924

距離分布関数 P(R)

ソフトウェア P(R): GNOM 5.0 / ポイント数: 953 /

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

結果

カーブのタイプ: extrapolated
コメント: 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.

	実験値	Porod
分子量	249.8 kDa	219 kDa
体積	-	351 nm3

	P(R)	Guinier	Guinier error
前方散乱 I0	90.51	92.63	0.5
慣性半径, Rg	4.02 nm	4.14 nm	0.03

	Min	Max
D	-	14.43
Guinier point	1	31