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Oxidoreductase PDB id
1crw
Jmol
Contents
Protein chains
333 a.a. *
Waters ×325
* Residue conservation analysis
PDB id:
1crw
Name: Oxidoreductase
Title: Crystal structure of apo-glyceraldehyde-3-phosphate dehydrog palinurus versicolor at 2.0a resolution
Structure: D-glyceraldehyde-3-phosphate-dehydrogenase. Chain: g, r. Ec: 1.2.1.12
Source: Palinurus versicolor. South china sea lobster. Organism_taxid: 82835. Tissue: tail muscle
Biol. unit: Tetramer (from PDB file)
Resolution:
2.00Å     R-factor:   0.165     R-free:   0.226
Authors: Y.Shen,J.Li,S.Song,Z.Lin
Key ref: Y.Q.Shen et al. (2000). Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor. J Struct Biol, 130, 1-9. PubMed id: 10806086 DOI: 10.1006/jsbi.2000.4220
Date:
16-Aug-99     Release date:   20-Sep-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P56649  (G3P_PANVR) -  Glyceraldehyde-3-phosphate dehydrogenase
Seq:
Struc:
333 a.a.
333 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.2.1.12  - Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Glyceraldehyde-3-phosphate Dehydrogenase (phosphorylating)
      Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate
+ phosphate
+ NAD(+)
= 3-phospho-D-glyceroyl phosphate
+ NADH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     nucleotide binding     6 terms  

 

 
    reference    
 
 
DOI no: 10.1006/jsbi.2000.4220 J Struct Biol 130:1-9 (2000)
PubMed id: 10806086  
 
 
Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor.
Y.Q.Shen, J.Li, S.Y.Song, Z.J.Lin.
 
  ABSTRACT  
 
d-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) shows cooperative properties for binding coenzymes. The structure of apo-GAPDH from Palinurus versicolor has been solved at 2.0 A resolution by X-ray crystallography. The final model gives a crystallographic R factor of 0.178 in the resolution range 8 to 2 A. The structural comparison with holo-GAPDH from the same species reveals a conformational change induced by coenzyme binding similar to that observed in Bacillus stearothermophilus GAPDH but to a lesser extent. The differences in magnitude during the apo-holo transition between these two enzymes were analyzed with respect to the change of the amino acid composition in the coenzyme binding pocket. In the crystalline state of apo-GAPDH, the overall structures of the subunits are similar to each other; however, significant differences in temperature factors and minor differences in domain rotation upon coenzyme binding were observed for different subunits. These structural features are discussed in relation to the environmental asymmetry of crystallographically independent subunits.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20164570 D.A.Butterfield, S.S.Hardas, and M.L.Lange (2010).
Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration.
  J Alzheimers Dis, 20, 369-393.  
16963457 F.Ferreira-da-Silva, P.J.Pereira, L.Gales, M.Roessle, D.I.Svergun, P.Moradas-Ferreira, and A.M.Damas (2006).
The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures.
  J Biol Chem, 281, 33433-33440.
PDB code: 2i5p
16510976 J.L.Jenkins, and J.J.Tanner (2006).
High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase.
  Acta Crystallogr D Biol Crystallogr, 62, 290-301.
PDB codes: 1u8f 2feh
16326908 V.F.Waingeh, C.D.Gustafson, E.I.Kozliak, S.L.Lowe, H.R.Knull, and K.A.Thomasson (2006).
Glycolytic enzyme interactions with yeast and skeletal muscle F-actin.
  Biophys J, 90, 1371-1384.  
14646080 S.W.Cowan-Jacob, M.Kaufmann, A.N.Anselmo, W.Stark, and M.G.Grütter (2003).
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase.
  Acta Crystallogr D Biol Crystallogr, 59, 2218-2227.
PDB code: 1j0x
12136140 Y.Q.Shen, S.Y.Song, and Z.J.Lin (2002).
Structures of D-glyceraldehyde-3-phosphate dehydrogenase complexed with coenzyme analogues.
  Acta Crystallogr D Biol Crystallogr, 58, 1287-1297.
PDB codes: 1ihx 1ihy
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.