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- SASDD29: Low load concentration of apo alpha-aminoadipic semialdehyde dehy... -

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Basic information

Entry
Database: SASBDB / ID: SASDD29
SampleLow load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS
  • Alpha-aminoadipic semialdehyde dehydrogenase (protein), ALDH7A1, Homo sapiens
Function / homology
Function and homology information


L-aminoadipate-semialdehyde dehydrogenase activity / L-aminoadipate-semialdehyde dehydrogenase / Choline catabolism / choline catabolic process / Lysine catabolism / betaine-aldehyde dehydrogenase (NAD+) activity / betaine-aldehyde dehydrogenase / glycine betaine biosynthetic process from choline / aldehyde metabolic process / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity ...L-aminoadipate-semialdehyde dehydrogenase activity / L-aminoadipate-semialdehyde dehydrogenase / Choline catabolism / choline catabolic process / Lysine catabolism / betaine-aldehyde dehydrogenase (NAD+) activity / betaine-aldehyde dehydrogenase / glycine betaine biosynthetic process from choline / aldehyde metabolic process / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity / aldehyde dehydrogenase (NAD+) / aldehyde dehydrogenase (NAD+) activity / sensory perception of sound / mitochondrial matrix / mitochondrion / extracellular exosome / identical protein binding / nucleus / cytosol
Similarity search - Function
Aldehyde dehydrogenase family 7 member A1-like / Aldehyde dehydrogenase, glutamic acid active site / Aldehyde dehydrogenases glutamic acid active site. / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, C-terminal / Aldehyde dehydrogenase, N-terminal / Aldehyde/histidinol dehydrogenase
Similarity search - Domain/homology
Alpha-aminoadipic semialdehyde dehydrogenase
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationJournal: FEBS Lett / Year: 2018
Title: NAD promotes assembly of the active tetramer of aldehyde dehydrogenase 7A1.
Authors: David A Korasick / Tommi A White / Srinivas Chakravarthy / John J Tanner /
Abstract: Nicotinamide adenine dinucleotide (NAD) is the redox cofactor of many enzymes, including the vast aldehyde dehydrogenase (ALDH) superfamily. Although the function of NAD(H) in hydride transfer is ...Nicotinamide adenine dinucleotide (NAD) is the redox cofactor of many enzymes, including the vast aldehyde dehydrogenase (ALDH) superfamily. Although the function of NAD(H) in hydride transfer is established, its influence on protein structure is less understood. Herein, we show that NAD -binding promotes assembly of the ALDH7A1 tetramer. Multiangle light scattering, small-angle X-ray scattering, and sedimentation velocity all show a pronounced shift of the dimer-tetramer equilibrium toward the tetramer when NAD is present. Furthermore, electron microscopy shows that cofactor binding enhances tetramer formation even at the low enzyme concentration used in activity assays, suggesting the tetramer is the active species. Altogether, our results suggest that the catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability.
Contact author
  • David Korasick (Mizzou, University of Missouri-Columbia, Columbia, MO, USA)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #2108
Type: atomic / Chi-square value: 1.15328552443
Search similar-shape structures of this assembly by Omokage search (details)
Model #2109
Type: atomic / Chi-square value: 0.984813013397
Search similar-shape structures of this assembly by Omokage search (details)
Model #2110
Type: atomic / Chi-square value: 0.984813013397
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Low load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS
BufferName: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol / pH: 7.8
Entity #1148Name: ALDH7A1 / Type: protein / Description: Alpha-aminoadipic semialdehyde dehydrogenase / Formula weight: 55.56 / Num. of mol.: 4 / Source: Homo sapiens / References: UniProt: P49419
Sequence: GHMSTLLINQ PQYAWLKELG LREENEGVYN GSWGGRGEVI TTYCPANNEP IARVRQASVA DYEETVKKAR EAWKIWADIP APKRGEIVRQ IGDALREKIQ VLGSLVSLEM GKILVEGVGE VQEYVDICDY AVGLSRMIGG PILPSERSGH ALIEQWNPVG LVGIITAFNF ...Sequence:
GHMSTLLINQ PQYAWLKELG LREENEGVYN GSWGGRGEVI TTYCPANNEP IARVRQASVA DYEETVKKAR EAWKIWADIP APKRGEIVRQ IGDALREKIQ VLGSLVSLEM GKILVEGVGE VQEYVDICDY AVGLSRMIGG PILPSERSGH ALIEQWNPVG LVGIITAFNF PVAVYGWNNA IAMICGNVCL WKGAPTTSLI SVAVTKIIAK VLEDNKLPGA ICSLTCGGAD IGTAMAKDER VNLLSFTGST QVGKQVGLMV QERFGRSLLE LGGNNAIIAF EDADLSLVVP SALFAAVGTA GQRCTTARRL FIHESIHDEV VNRLKKAYAQ IRVGNPWDPN VLYGPLHTKQ AVSMFLGAVE EAKKEGGTVV YGGKVMDRPG NYVEPTIVTG LGHDASIAHT ETFAPILYVF KFKNEEEVFA WNNEVKQGLS SSIFTKDLGR IFRWLGPKGS DCGIVNVNIP TSGAEIGGAF GGEKHTGGGR ESGSDAWKQY MRRSTCTINY SKDLPLAQGI KFQ

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Experimental information

BeamInstrument name: Advanced Photon Source (APS) BioCAT 18ID / City: Argonne, IL / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.103 Å / Dist. spec. to detc.: 3.5 mm
DetectorName: Pilatus 100K / Pixsize x: 172 mm
Scan
Title: Low load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS
Measurement date: Feb 22, 2018 / Cell temperature: 22 °C / Exposure time: 0.5 sec. / Unit: 1/A /
MinMax
Q0.0081 0.387
ResultType of curve: sec
Comments: Column type: Wyatt WTC 030 S5; flow rate: 0.8 mL/min; injection volume: 250 - 500 µL
ExperimentalPorod
MW100.4 kDa-
Volume-212 nm3

GuinierGuinier error
Forward scattering, I042.4 0.4
Radius of gyration, Rg3.47 nm0.05

MinMax
Guinier point1 98

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