Document Detail


Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: reversible decamer assembly controls enzyme activity.
MedLine Citation:
PMID:  19298070     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Juni Andréll; Matthew G Hicks; Tracy Palmer; Elisabeth P Carpenter; So Iwata; Megan J Maher
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  48     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-05-05     Completed Date:  2009-06-09     Revised Date:  2014-02-19    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3915-27     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acids / 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:
G117/519//Medical Research Council; //Biotechnology and Biological Sciences Research Council; //Medical Research Council
Chemical
Reg. No./Substance:
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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