PDBsum entry 1ee9

Oxidoreductase

PDB id: 1ee9

Contents

Protein chain

317 a.a. *

Ligands

NAD

Waters ×6

* Residue conservation analysis

PDB id:

1ee9

Name:

Oxidoreductase

Title:

Crystal structure of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from saccharomyces cerevisiae complexed with NAD

Structure:

5,10-methylenetetrahydrofolate dehydrogenase. Chain: a. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PDB file)

Resolution:

3.00Å R-factor: 0.248 R-free: 0.360

Authors:

A.F.Monzingo,A.Breksa,S.Ernst,D.R.Appling,J.D.Robertus

Key ref:

A.F.Monzingo et al. (2000). The X-ray structure of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae. Protein Sci, 9, 1374-1381. PubMed id: 10933503 DOI: 10.1110/ps.9.7.1374

Date:

31-Jan-00 Release date: 06-Dec-00

Protein chain

Q02046  (MTD1_YEAST) -  Methylenetetrahydrofolate dehydrogenase [NAD(+)] from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 320 a.a.

Struc: 317 a.a.

Enzyme reactions

• Enzyme class: E.C.1.5.1.15 - methylenetetrahydrofolate dehydrogenase (NAD(+)).
• Pathway: Folate Coenzymes
• Reaction: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD⁺ = (6R)-5,10- methenyltetrahydrofolate + NADH

(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) (Bound ligand (Het Group name = NAD) corresponds exactly) = (6R)-5,10- methenyltetrahydrofolate + NADH

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1110/ps.9.7.1374

Protein Sci 9:1374-1381 (2000)

PubMed id: 10933503

The X-ray structure of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae.

A.F.Monzingo, A.Breksa, S.Ernst, D.R.Appling, J.D.Robertus.

ABSTRACT

Eucaryotes possess one or more NADP-dependent methylene-THF dehydrogenases as part of multifunctional enzymes. In addition, yeast expresses an unusual monofunctional NAD-dependent enzyme, yMTD. We report X-ray structures for the apoenzyme and its complex with NAD+ at 2.8 and 3.0 A resolution, respectively. The protein fold resembles that seen for the human and Escherichia coli dehydrogenase/cyclohydrolase bifunctional enzymes. The enzyme has two prominent domains, with the active site cleft between them. yMTD has a noncanonical NAD-binding domain that has two inserted strands compared with the NADP-binding domains of the bifunctional enzymes. This insert precludes yMTD from dimerizing in the same way as the bifunctional enzymes. yMTD functions as a dimer, but the mode of dimerization is novel. It does not appear that the difference in dimerization accounts for the difference in cofactor specificity or for the loss of cyclohydrolase activity. These functional differences are probably accounted for by minor differences within the tertiary structure of the active site of the monomeric protein.