| Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: reversible decamer assembly controls enzyme activity. | |
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MedLine Citation:
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PMID: 19298070 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The acid-induced arginine decarboxylase is part of an enzymatic system in Escherichia coli that contributes to making this organism acid resistant. The arginine decarboxylase is a vitamin B(6)-dependent enzyme that is active at acidic pH. It consumes a proton in the decarboxylation of arginine to agmatine, and by working in tandem with an arginine-agmatine antiporter, this enzymatic cycle protects the organism by preventing the accumulation of protons inside the cell. We have determined the structure of the acid-induced arginine decarboxylase by X-ray crystallography to 2.4 A resolution. The arginine decarboxylase structure revealed a ca. 800 kDa decamer composed as a pentamer of five homodimers. Each homodimer has an abundance of acidic surface residues, which at neutral pH prevents inactive homodimers from associating into active decamers. Conversely, acidic conditions favor the assembly of active decamers. Therefore, the structure of arginine decarboxylase presents a mechanism by which its activity is modulated by external pH. |
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Authors:
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Juni Andréll; Matthew G Hicks; Tracy Palmer; Elisabeth P Carpenter; So Iwata; Megan J Maher |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemistry Volume: 48 ISSN: 1520-4995 ISO Abbreviation: Biochemistry Publication Date: 2009 May |
Date Detail:
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Created Date: 2009-05-05 Completed Date: 2009-06-09 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 3915-27 Citation Subset: IM |
Affiliation:
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Division of Molecular Biosciences, Imperial College, London SW7 2AZ, UK. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acids
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pharmacology* Biopolymers / biosynthesis, chemistry Carboxy-Lyases / biosynthesis, chemistry* Crystallography, X-Ray Enzyme Induction Escherichia coli / enzymology* Hydrogen-Ion Concentration Models, Molecular Protein Conformation |
| Grant Support | |
ID/Acronym/Agency:
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//Biotechnology and Biological Sciences Research Council; //Medical Research Council |
| Chemical | |
Reg. No./Substance:
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0/Acids; 0/Biopolymers; EC 4.1.1.-/Carboxy-Lyases; EC 4.1.1.19/arginine decarboxylase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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