The Crystal and Solution Structures of Glyceraldehyde-3-phosphate Dehydrogenase Reveal Different Quaternary Structures

Ferreira-da-Silva F, Pereira P, Gales L, Roessle M, Svergun D, Moradas-Ferreira P, Damas A
Journal of Biological Chemistry 281(44):33433-33440 (2006 Nov)

doi: 10.1074/jbc.M605267200
Submitted to SASBDB: 2021 Dec 14
Published in SASBDB:

SASDN92 – Apoform of glyceraldehyde-3-phosphate dehydrogenase (apo-kmGAPDH1p)

Glyceraldehyde-3-phosphate dehydrogenase 1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Glyceraldehyde-3-phosphate dehydrogenase 1 tetramer, 142 kDa Kluyveromyces marxianus protein
Buffer: 150 mM NaCl, 1 mM beta-mercaptoethanol, 1 mM EDTA, 10 mM TrisHCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Mar 27
RgGuinier 4.2 nm
Dmax 12.0 nm
VolumePorod 234 nm3

SASDNA2 – Glyceraldehyde-3-phosphate dehydrogenase (apo-kmGAPDH1p) upon NAD+ binding

Glyceraldehyde-3-phosphate dehydrogenase 1 bound to NAD+ experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Glyceraldehyde-3-phosphate dehydrogenase 1 bound to NAD+ tetramer, 142 kDa Kluyveromyces marxianus protein
Buffer: 150 mM NaCl, 1 mM beta-mercaptoethanol, 1 mM EDTA, 10 mM TrisHCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Mar 27
RgGuinier 3.7 nm
Dmax 9.9 nm
VolumePorod 202 nm3