Publication Date:
2006-02-18
Description:
Numerous microorganisms oxidize sulfur for energy conservation and contribute to the global biogeochemical sulfur cycle. We have determined the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes an oxygen-dependent disproportionation of elemental sulfur. Twenty-four monomers form a large hollow sphere enclosing a positively charged nanocompartment. Apolar channels provide access for linear sulfur species. A cysteine persulfide and a low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitute the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Urich, Tim -- Gomes, Claudio M -- Kletzin, Arnulf -- Frazao, Carlos -- New York, N.Y. -- Science. 2006 Feb 17;311(5763):996-1000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Darmstadt University of Technology, Institute of Microbiology and Genetics, Schnittspahnstrasse 10, 64287 Darmstadt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16484493" target="_blank"〉PubMed〈/a〉
Keywords:
Acidianus/*enzymology/physiology
;
Amino Acid Sequence
;
Archaeal Proteins/*chemistry/metabolism
;
Binding Sites
;
Catalysis
;
Catalytic Domain
;
Crystallization
;
Crystallography, X-Ray
;
Hot Temperature
;
Hydrophobic and Hydrophilic Interactions
;
Iron/chemistry/metabolism
;
Ligands
;
Models, Molecular
;
Molecular Sequence Data
;
Oxidation-Reduction
;
Oxidoreductases Acting on Sulfur Group Donors/*chemistry/metabolism
;
Protein Conformation
;
Protein Folding
;
Protein Structure, Quaternary
;
Protein Structure, Tertiary
;
Recombinant Proteins/chemistry
;
Static Electricity
;
Sulfur/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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