1DSS

STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR

Summary for 1DSS

• Entry DOI: 10.2210/pdb1dss/pdb
• Descriptor: D-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: active-site carboxymethylation, d-glyceraldehyde-3-phosphate-dehydrogenase, 'the-half-of-sites' reaction, molecular symmetry
• Biological source: Palinurus versicolor (South China Sea lobster)
• Cellular location: Cytoplasm: P56649
• Total number of polymer chains: 2
• Total formula weight: 73361.18

Authors

Song, S.,Lin, Z. (deposition date: 1997-06-04, release date: 1998-12-09, Last modification date: 2024-04-03)

Primary citation

Song, S.Y.,Xu, Y.B.,Lin, Z.J.,Tsou, C.L.
Structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor.
J.Mol.Biol., 287:719-725, 1999

PubMed Abstract: The structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor was determined in the presence of coenzyme NAD+ at 1.88 A resolution with a final R-factor of 0.175. The structure refinement was carried out on the basis of the structure of holo-GAPDH at 2.0 A resolution using the program XPLOR. The carboxymethyl group connected to Cys149 is stabilized by a hydrogen bond between its OZ1 and Cys149N, and charge interaction between the carboxyl group and the nicotinamide moiety. The modification of Cys149 induced conformational changes in the active site, in particular, the site of sulphate ion 501 (the proposed attacking inorganic phosphate ion in catalysis), and segment 208-218 nearby. Extensive hydrogen-bonding interactions occur in the active site, which contribute to the higher stability of the modified enzyme. The modification of the active site did not affect the conformation of GAPDH elsewhere, including the subunit interfaces. The structures of the green and red subunits in the asymmetric unit are nearly identical, suggesting that the half-site reactivity of this enzyme is from ligand-induced rather than pre-existing asymmetry. It is proposed that the carboxymethyl group takes the place of the acyl group of the reaction intermediate, and the catalytic mechanism of this enzyme is discussed in the light of a comparison of the structures of the native and the carboxymethylated GAPDH.

PubMed: 10191140
DOI: 10.1006/jmbi.1999.2628

Experimental method

X-RAY DIFFRACTION (1.88 Å)