1dgj
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1dgj.jpg|left|200px]] | [[Image:1dgj.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1dgj", 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_1dgj| PDB=1dgj | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774''' | '''CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774''' | ||
| Line 30: | Line 27: | ||
[[Category: Rebelo, J M.]] | [[Category: Rebelo, J M.]] | ||
[[Category: Romao, M J.]] | [[Category: Romao, M J.]] | ||
| - | [[Category: | + | [[Category: Beta barrel]] |
| - | [[Category: | + | [[Category: Beta half-barrel]] |
| - | [[Category: | + | [[Category: Four-helix bundle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:50:01 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:50, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 13:50:01 2008
