1dgj
From Proteopedia
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|PDB= 1dgj |SIZE=350|CAPTION= <scene name='initialview01'>1dgj</scene>, resolution 2.8Å | |PDB= 1dgj |SIZE=350|CAPTION= <scene name='initialview01'>1dgj</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=2MO:MOLYBDENUM+(IV)OXIDE+ION'>2MO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MCN:PTERIN+CYTOSINE+DINUCLEOTIDE'>MCN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1alo|1alo]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgj OCA], [http://www.ebi.ac.uk/pdbsum/1dgj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dgj RCSB]</span> | ||
}} | }} | ||
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[[Category: Rebelo, J M.]] | [[Category: Rebelo, J M.]] | ||
[[Category: Romao, M J.]] | [[Category: Romao, M J.]] | ||
| - | [[Category: 2MO]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: MCN]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: beta half-barrel]] | [[Category: beta half-barrel]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:15 2008'' |
Revision as of 16:41, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1alo
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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