1ee9
From Proteopedia
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| - | [[Image:1ee9.jpg|left|200px]] | + | [[Image:1ee9.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH NAD''' | + | {{Structure |
| + | |PDB= 1ee9 |SIZE=350|CAPTION= <scene name='initialview01'>1ee9</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH NAD''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EE9 is a [ | + | 1EE9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EE9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10933503 10933503] |
[[Category: Methylenetetrahydrofolate dehydrogenase (NAD(+))]] | [[Category: Methylenetetrahydrofolate dehydrogenase (NAD(+))]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: protein-nad complex]] | [[Category: protein-nad complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:54:27 2008'' |
Revision as of 08:54, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Methylenetetrahydrofolate dehydrogenase (NAD(+)), with EC number 1.5.1.15 | ||||||
| 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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