1ys4
From Proteopedia
(New page: 200px<br /><applet load="1ys4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ys4, resolution 2.29Å" /> '''Structure of Asparta...) |
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| - | [[Image:1ys4.jpg|left|200px]]<br /><applet load="1ys4" size=" | + | [[Image:1ys4.jpg|left|200px]]<br /><applet load="1ys4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ys4, resolution 2.29Å" /> | caption="1ys4, resolution 2.29Å" /> | ||
'''Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii'''<br /> | '''Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of aspartate-beta-semialdehyde dehydrogenase (ASADH) from | + | The structure of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Methanococcus jannaschii has been determined to 2.3 angstroms resolution using multiwavelength anomalous diffraction (MAD) phasing of a selenomethionine-substituted derivative to define a new branch in the family of ASADHs. This new structure has a similar overall fold and domain organization despite less than 10% conserved sequence identity with the bacterial enzymes. However, the entire repertoire of functionally important active site amino acid residues is conserved, suggesting an identical catalytic mechanism but with lower catalytic efficiency. A new coenzyme-binding conformation and dual NAD/NADP coenzyme specificity further distinguish this archaeal branch from the bacterial ASADHs. Several structural differences are proposed to account for the dramatically enhanced thermostability of this archaeal enzyme. Finally, the intersubunit communication channel connecting the active sites in the bacterial enzyme dimer has been disrupted in the archaeal ASADHs by amino acid changes that likely prevent the alternating sites reactivity previously proposed for the bacterial ASADHs. |
==About this Structure== | ==About this Structure== | ||
| - | 1YS4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with NAP and MLA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] Full crystallographic information is available from [http:// | + | 1YS4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=MLA:'>MLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YS4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Faehnle, C | + | [[Category: Faehnle, C R.]] |
| - | [[Category: Ohren, J | + | [[Category: Ohren, J F.]] |
| - | [[Category: Viola, R | + | [[Category: Viola, R E.]] |
[[Category: MLA]] | [[Category: MLA]] | ||
[[Category: NAP]] | [[Category: NAP]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:33 2008'' |
Revision as of 14:08, 21 February 2008
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Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii
Overview
The structure of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Methanococcus jannaschii has been determined to 2.3 angstroms resolution using multiwavelength anomalous diffraction (MAD) phasing of a selenomethionine-substituted derivative to define a new branch in the family of ASADHs. This new structure has a similar overall fold and domain organization despite less than 10% conserved sequence identity with the bacterial enzymes. However, the entire repertoire of functionally important active site amino acid residues is conserved, suggesting an identical catalytic mechanism but with lower catalytic efficiency. A new coenzyme-binding conformation and dual NAD/NADP coenzyme specificity further distinguish this archaeal branch from the bacterial ASADHs. Several structural differences are proposed to account for the dramatically enhanced thermostability of this archaeal enzyme. Finally, the intersubunit communication channel connecting the active sites in the bacterial enzyme dimer has been disrupted in the archaeal ASADHs by amino acid changes that likely prevent the alternating sites reactivity previously proposed for the bacterial ASADHs.
About this Structure
1YS4 is a Single protein structure of sequence from Methanocaldococcus jannaschii with and as ligands. Active as Aspartate-semialdehyde dehydrogenase, with EC number 1.2.1.11 Full crystallographic information is available from OCA.
Reference
A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii., Faehnle CR, Ohren JF, Viola RE, J Mol Biol. 2005 Nov 11;353(5):1055-68. Epub 2005 Sep 29. PMID:16225889
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