1B0A

5,10, METHYLENE-TETRAHYDROPHOLATE DEHYDROGENASE/CYCLOHYDROLASE FROM E COLI.

Summary for 1B0A

• Entry DOI: 10.2210/pdb1b0a/pdb
• Descriptor: PROTEIN (FOLD BIFUNCTIONAL PROTEIN) (2 entities in total)
• Functional Keywords: folate, dehydrogenase, cyclcohydrolase, bifunctional, channeling, oxidoreductase, hydrolase
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 31078.67

Authors

Shen, B.W.,Dyer, D.,Huang, J.-Y.,D'Ari, L.,Rabinowitz, J.,Stoddard, B.L. (deposition date: 1998-11-06, release date: 1999-06-29, Last modification date: 2023-12-27)

Primary citation

Shen, B.W.,Dyer, D.H.,Huang, J.Y.,D'Ari, L.,Rabinowitz, J.,Stoddard, B.L.
The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase.
Protein Sci., 8:1342-1349, 1999

PubMed Abstract: The structure of a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/cyclohydrolase from Escherichia coli has been determined at 2.5 A resolution in the absence of bound substrates and compared to the NADP-bound structure of the homologous enzyme domains from a trifunctional human synthetase enzyme. Superposition of these structures allows the identification of a highly conserved cluster of basic residues that are appropriately positioned to serve as a binding site for the poly-gamma-glutamyl tail of the tetrahydrofolate substrate. Modeling studies and molecular dynamic simulations of bound methylene-tetrahydrofolate and NADP shows that this binding site would allow interaction of the nicotinamide and pterin rings in the dehydrogenase active site. Comparison of these enzymes also indicates differences between their active sites that might allow the development of inhibitors specific to the bacterial target.

PubMed: 10386884

Experimental method

X-RAY DIFFRACTION (2.56 Å)