THE STRUCTURE OF LOBSTER APO-D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 3.0 ANGSTROMS RESOLUTION

Structure of lobster apo-D-glyceraldehyde-3-phosphate dehydrogenase at 3.0 A resolution.

Studies of Asymmetry in the Three-Dimensional Structure of Lobster D-Glyceraldehyde-3-Phosphate Dehydrogenase

Anion Binding Sites in the Active Center of D-Glyceraldehyde-3-Phosphate Dehydrogenase

Studies on Coenzyme Binding to Glyceraldehyde-3-Phosphate Dehydrogenase

STRUCTURE AND CONFORMATION OF NUCLEIC ACIDS AND PROTEIN-NUCLEIC ACID INTERACTIONS : PROCEEDINGS OF THE FOURTH ANNUAL HARRY STEENBOCK SYMPOSIUM, JUNE 16-19, 1974, MADISON, WISCONSIN
A Comparison of the Binding and Function of Nad with Respect to Lactate Dehydrogenase and Glyceraldehyde-3-Phosphate Dehydrogenase

Sequence Variability and Structure of D-Glyceraldehyde-3-Phosphate Dehydrogenase

Three-Dimensional Structure of D-Glyceraldehyde-3-Phosphate Dehydrogenase

Structure Determination of Crystalline Lobster D-Glyceraldehyde-3-Phosphate Dehydrogenase

D-Glyceraldehyde-3-Phosphate Dehydrogenase, Three-Dimensional Structure and Evolutionary Significance

An Application of the Molecular Replacement Technique in Direct Space to a Known Protein Structure

APO-D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

SKIGINGFGRIGRLVLRAALSCGAQVVAVNDPFIALEYMVYMFKYDSTHGVFKGEVKMEDGALVVDGKKITVFNEMKPEN
IPWSKAGAEYIVESTGVFTTIEKASAHFKGGAKKVVISAPSADAPMFVCGVNLEKYSKDMTVVSNASCTTNCLAPVAKVL
HENFEIVEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELDGKLTGMAFRVPTPDVSVVD
LTVRLGKECSYDDIKAAMKTASEGPLQGFLGYTEDDVVSSDFIGDNRSSIFDAKAGIQLSKTFVKVVSWYDNEFGYSQRV
IDLLKHMQKVDSA

SHEET
THE SHEET SUBSTRUCTURE OF THE CATALYTIC DOMAIN IS
BIFURCATED. TO REPRESENT THIS FEATURE REDUNDANT SHEETS
ARE DEFINED. STRANDS 1-7 OF SHEET C1 ARE IDENTICAL TO
STRANDS 1-7 OF SHEET C2.

EACH SUBUNIT IS CONSIDERED TO BE COMPRISED OF A COFACTOR BINDING DOMAIN AND A CATALYTIC DOMAIN. THE CHARACTERS B AND C IN THE SHEET IDENTIFIERS ARE USED TO DENOTE WHICH DOMAIN INCLUDES THESE STRUCTURAL FEATURES.
THE SEQUENCE GIVEN IN *PIR* SHOWS RESIDUE 6 TO BE ASP. THE DATA PRESENTED IN THIS ENTRY SHOWS RESIDUE 6 AS ASN (M. ROSSMANN, PRIVATE COMMUNICATION FROM J. HARRIS).

THE PHASES FOR APO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE WERE DERIVED BY THE MOLECULAR REPLACEMENT TECHNIQUE. THE INITIAL PHASING MODEL WAS THE HOLO GAPDH ELECTRON DENSITY SUITABLY TRANSFORMED TO THE TRICLINIC APO GAPDH CELL. THE KNOWN 222 SYMMETRY OF THE TETRAMERIC MOLECULE WAS USED IN IMPROVING THE PHASES BY ELECTRON DENSITY AVERAGING. THE STRUCTURE WAS FOUND TO BE VERY SIMILAR TO THAT OF THE HOLO ENZYME.

THE TRANSFORMATION PRESENTED AS *MTRIX 1* BELOW WILL YIELD
APPROXIMATE COORDINATES FOR CHAIN 2 WHEN APPLIED TO CHAIN
1. THE TRANSFORMATION PRESENTED AS *MTRIX 2* BELOW WILL
YIELD APPROXIMATE COORDINATES FOR CHAIN 3 WHEN APPLIED TO
CHAIN 1. THE TRANSFORMATION PRESENTED AS *MTRIX 3* BELOW
WILL YIELD APPROXIMATE COORDINATES FOR CHAIN 4 WHEN APPLIED
TO CHAIN 1.

RESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR

RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR

RESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR.

RESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR

RESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR