1edz: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1edz.gif|left|200px]] | [[Image:1edz.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1edz", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1edz| PDB=1edz | SCENE= }} | ||
}} | |||
'''STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE''' | '''STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE''' | ||
| Line 23: | Line 20: | ||
==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://www.ncbi.nlm.nih.gov/pubmed/10933503 10933503] | 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: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 31: | Line 27: | ||
[[Category: Monzingo, A F.]] | [[Category: Monzingo, A F.]] | ||
[[Category: Robertus, J D.]] | [[Category: Robertus, J D.]] | ||
[[Category: | [[Category: Dehydrogenase]] | ||
[[Category: | [[Category: Folate]] | ||
[[Category: | [[Category: Monofunctional]] | ||
[[Category: | [[Category: Nucleotide-binding domain]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:58:48 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 14:58, 2 May 2008
STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE
OverviewOverview
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 StructureAbout this Structure
1EDZ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 14:58:48 2008