1GPD

STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Summary for 1GPD

• Entry DOI: 10.2210/pdb1gpd/pdb
• Descriptor: D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: oxido-reductase(aldehyde/donr, nad/accpt), oxido-reductase(aldehyde-donr, nad-accpt) complex, oxidoreductase
• Biological source: Homarus americanus (American lobster)
• Cellular location: Cytoplasm: P00357
• Total number of polymer chains: 2
• Total formula weight: 73274.63

Authors

Moras, D.,Olsen, K.W.,Sabesan, M.N.,Buehner, M.,Ford, G.C.,Rossmann, M.G. (deposition date: 1975-07-01, release date: 1977-02-17, Last modification date: 2024-10-30)

Primary citation

Moras, D.,Olsen, K.W.,Sabesan, M.N.,Buehner, M.,Ford, G.C.,Rossmann, M.G.
Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase.
J.Biol.Chem., 250:9137-9162, 1975

PubMed Abstract: An improved electron density map of lobster holo-D-glyceraldehyde-3-phosphate dehydrogenase has been computed to 2.9 A resolution based on two heavy atom isomorphous derivatives. This has been averaged only over the Q molecular 2-fold axis, which is known to be exact in the human holoenzyme. The map showed possible asymmetry between the subunits in which the active centers are closely related across the R axis (that is, between the red and green or between the yellow and blue subunits). A difference map between the electron density of citrate and sulfate-soaked crystals gave further evidence for possible asymmetry. The major differences of electron density between R axis-related subunits appear around the active center and suggest the following interpretations. 1. The conformation of the adenine about the glycosidic bond is the more frequently observed anti with a C-2' endo conformation for the ribose ring in the red and yellow subunits, but is probably syn with a C-3' endo conformation in the green and blue subunits.2. The adenine ribose has its 3'-hydroxyl group hydrogen-bonded to a main chain carbonyl group in the red and yellow subunits but not in the green and blue subunits, as a consequence of the differing ribose conformations. 3. Cysteine-149 is more closely associated with histidine-176 in the green and blue subunits, and appears nearer the nicotinamide in the red and yellow subunits.

PubMed: 127793

Experimental method

X-RAY DIFFRACTION (2.9 Å)