<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Romao, M. J.</style></author><author><style face="normal" font="default" size="100%">Archer, M.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Legall, J.</style></author><author><style face="normal" font="default" size="100%">Engh, R.</style></author><author><style face="normal" font="default" size="100%">Schneider, M.</style></author><author><style face="normal" font="default" size="100%">Hof, P.</style></author><author><style face="normal" font="default" size="100%">Huber, R.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas</style></title><secondary-title><style face="normal" font="default" size="100%">Science</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aldehyde Oxidoreductases/*chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Coenzymes/chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallization</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallography, X-Ray</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytosine Nucleotides/chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/*enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Drosophila melanogaster/enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen Bonding</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">Metalloproteins/chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Molybdenum/chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Folding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Secondary</style></keyword><keyword><style  face="normal" font="default" size="100%">Pteridines/chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Pterins/chemistry/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Xanthine</style></keyword><keyword><style  face="normal" font="default" size="100%">Xanthine Oxidase/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Xanthines/metabolism</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Nov 17</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=7502041 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">5239</style></number><volume><style face="normal" font="default" size="100%">270</style></volume><pages><style face="normal" font="default" size="100%">1170-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The crystal structure of the aldehyde oxido-reductase (Mop) from the sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas has been determined at 2.25 A resolution by multiple isomorphous replacement and refined. The protein, a homodimer of 907 amino acid residues subunits, is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centers. It is folded into four domains of which the first two bind the iron sulfur centers and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">7502041</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0036-8075 (Print)0036-8075 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Instituto de Tecnologia Quimica e Biologica, Oeiras, Portugal.</style></auth-address></record></records></xml>