1ee9
From Proteopedia
(New page: 200px<br /><applet load="1ee9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ee9, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ee9.jpg|left|200px]]<br /><applet load="1ee9" size=" | + | [[Image:1ee9.jpg|left|200px]]<br /><applet load="1ee9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ee9, resolution 3.0Å" /> | caption="1ee9, resolution 3.0Å" /> | ||
'''CRYSTAL STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH NAD'''<br /> | '''CRYSTAL STRUCTURE OF THE NAD-DEPENDENT 5,10-METHYLENETETRAHYDROFOLATE DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH NAD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Eucaryotes possess one or more NADP-dependent methylene-THF dehydrogenases | + | 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== | ==About this Structure== | ||
| - | 1EE9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1EE9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EE9 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Appling, D | + | [[Category: Appling, D R.]] |
[[Category: Breksa, A.]] | [[Category: Breksa, A.]] | ||
[[Category: Ernst, S.]] | [[Category: Ernst, S.]] | ||
| - | [[Category: Monzingo, A | + | [[Category: Monzingo, A F.]] |
| - | [[Category: Robertus, J | + | [[Category: Robertus, J D.]] |
[[Category: NAD]] | [[Category: NAD]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
| Line 27: | Line 27: | ||
[[Category: protein-nad complex]] | [[Category: protein-nad complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:59 2008'' |
Revision as of 10:27, 21 February 2008
|
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 with as ligand. Active as Methylenetetrahydrofolate dehydrogenase (NAD(+)), with EC number 1.5.1.15 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
Page seeded by OCA on Thu Feb 21 12:26:59 2008
