1dgj
From Proteopedia
(New page: 200px<br /><applet load="1dgj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dgj, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1dgj.jpg|left|200px]]<br /><applet load="1dgj" size=" | + | [[Image:1dgj.jpg|left|200px]]<br /><applet load="1dgj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dgj, resolution 2.8Å" /> | caption="1dgj, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774'''<br /> | '''CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The aldehyde oxidoreductase (MOD) isolated from the sulfate reducer | + | The aldehyde oxidoreductase (MOD) isolated from the sulfate reducer Desulfovibrio desulfuricans (ATCC 27774) is a member of the xanthine oxidase family of molybdenum-containing enzymes. It has substrate specificity similar to that of the homologous enzyme from Desulfovibrio gigas (MOP) and the primary sequences from both enzymes show 68 % identity. The enzyme was crystallized in space group P6(1)22, with unit cell dimensions of a=b=156.4 A and c=177.1 A, and diffraction data were obtained to beyond 2.8 A. The crystal structure was solved by Patterson search techniques using the coordinates of the D. gigas enzyme. The overall fold of the D. desulfuricans enzyme is very similar to MOP and the few differences are mapped to exposed regions of the molecule. This is reflected in the electrostatic potential surfaces of both homologous enzymes, one exception being the surface potential in a region identifiable as the putative docking site of the physiological electron acceptor. Other essential features of the MOP structure, such as residues of the active-site cavity, are basically conserved in MOD. Two mutations are located in the pocket bearing a chain of catalytically relevant water molecules.As deduced from this work, both these enzymes are very closely related in terms of their sequences as well as 3D structures. The comparison allowed confirmation and establishment of features that are essential for their function; namely, conserved residues in the active-site, catalytically relevant water molecules and recognition of the physiological electron acceptor docking site. |
==About this Structure== | ==About this Structure== | ||
| - | 1DGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with FES, 2MO and MCN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=2MO:'>2MO</scene> and <scene name='pdbligand=MCN:'>MCN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Desulfovibrio desulfuricans]] | [[Category: Desulfovibrio desulfuricans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dias, J | + | [[Category: Dias, J M.]] |
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Macieira, S.]] | [[Category: Macieira, S.]] | ||
| - | [[Category: Rebelo, J | + | [[Category: Rebelo, J M.]] |
| - | [[Category: Romao, M | + | [[Category: Romao, M J.]] |
[[Category: 2MO]] | [[Category: 2MO]] | ||
[[Category: FES]] | [[Category: FES]] | ||
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[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:27 2008'' |
Revision as of 10:16, 21 February 2008
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CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774
Overview
The aldehyde oxidoreductase (MOD) isolated from the sulfate reducer Desulfovibrio desulfuricans (ATCC 27774) is a member of the xanthine oxidase family of molybdenum-containing enzymes. It has substrate specificity similar to that of the homologous enzyme from Desulfovibrio gigas (MOP) and the primary sequences from both enzymes show 68 % identity. The enzyme was crystallized in space group P6(1)22, with unit cell dimensions of a=b=156.4 A and c=177.1 A, and diffraction data were obtained to beyond 2.8 A. The crystal structure was solved by Patterson search techniques using the coordinates of the D. gigas enzyme. The overall fold of the D. desulfuricans enzyme is very similar to MOP and the few differences are mapped to exposed regions of the molecule. This is reflected in the electrostatic potential surfaces of both homologous enzymes, one exception being the surface potential in a region identifiable as the putative docking site of the physiological electron acceptor. Other essential features of the MOP structure, such as residues of the active-site cavity, are basically conserved in MOD. Two mutations are located in the pocket bearing a chain of catalytically relevant water molecules.As deduced from this work, both these enzymes are very closely related in terms of their sequences as well as 3D structures. The comparison allowed confirmation and establishment of features that are essential for their function; namely, conserved residues in the active-site, catalytically relevant water molecules and recognition of the physiological electron acceptor docking site.
About this Structure
1DGJ is a Single protein structure of sequence from Desulfovibrio desulfuricans with , and as ligands. Full crystallographic information is available from OCA.
Reference
Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774., Rebelo J, Macieira S, Dias JM, Huber R, Ascenso CS, Rusnak F, Moura JJ, Moura I, Romao MJ, J Mol Biol. 2000 Mar 17;297(1):135-46. PMID:10704312
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