1ee9
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_dehydrogenase_(NAD(+)) Methylenetetrahydrofolate dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.15 1.5.1.15] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_dehydrogenase_(NAD(+)) Methylenetetrahydrofolate dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.15 1.5.1.15] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1edz|1EDZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ee9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ee9 OCA], [http://www.ebi.ac.uk/pdbsum/1ee9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ee9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Monzingo, A F.]] | [[Category: Monzingo, A F.]] | ||
[[Category: Robertus, J D.]] | [[Category: Robertus, J D.]] | ||
| - | [[Category: NAD]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
[[Category: folate]] | [[Category: folate]] | ||
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[[Category: protein-nad complex]] | [[Category: protein-nad complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:00:52 2008'' |
Revision as of 17:00, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Methylenetetrahydrofolate dehydrogenase (NAD(+)), with EC number 1.5.1.15 | ||||||
| Related: | 1EDZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH NAD
Overview
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.
About this Structure
1EE9 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The X-ray structure of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae., Monzingo AF, Breksa A, Ernst S, Appling DR, Robertus JD, Protein Sci. 2000 Jul;9(7):1374-81. PMID:10933503
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