Publication Date:
1995-11-17
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Romao, M J -- Archer, M -- Moura, I -- Moura, J J -- LeGall, J -- Engh, R -- Schneider, M -- Hof, P -- Huber, R -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1170-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto de Tecnologia Quimica e Biologica, Oeiras, Portugal.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502041" target="_blank"〉PubMed〈/a〉
Keywords:
Aldehyde Oxidoreductases/*chemistry/metabolism
;
Amino Acid Sequence
;
Animals
;
Coenzymes/chemistry/metabolism
;
Crystallization
;
Crystallography, X-Ray
;
Cytosine Nucleotides/chemistry/metabolism
;
Desulfovibrio/*enzymology
;
Drosophila melanogaster/enzymology
;
Electron Transport
;
Hydrogen Bonding
;
Iron/chemistry
;
Ligands
;
Metalloproteins/chemistry/metabolism
;
Molecular Sequence Data
;
Molybdenum/chemistry/metabolism
;
Oxidation-Reduction
;
Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
;
Pteridines/chemistry/metabolism
;
Pterins/chemistry/metabolism
;
Xanthine
;
Xanthine Oxidase/*chemistry
;
Xanthines/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
