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2VYC

Crystal Structure of Acid Induced Arginine Decarboxylase from E. coli

Summary for 2VYC
Entry DOI10.2210/pdb2vyc/pdb
DescriptorBIODEGRADATIVE ARGININE DECARBOXYLASE, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
Functional Keywordsarginine decarboxylase, pyridoxal phosphate, plp-dependent enzyme, lyase, decarboxylase, acid resistance
Biological sourceESCHERICHIA COLI
Cellular locationCytoplasm: P28629
Total number of polymer chains10
Total formula weight847592.04
Authors
Andrell, J.,Hicks, M.G.,Palmer, T.,Carpenter, E.P.,Iwata, S.,Maher, M.J. (deposition date: 2008-07-22, release date: 2009-03-31, Last modification date: 2025-04-09)
Primary citationAndrell, J.,Hicks, M.G.,Palmer, T.,Carpenter, E.P.,Iwata, S.,Maher, M.J.
Crystal Structure of the Acid Induced Arginine Decarboxylase from Escherichia Coli: Reversible Decamer Assembly Controls Enzyme Activity.
Biochemistry, 48:3915-, 2009
Cited by
PubMed Abstract: 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.
PubMed: 19298070
DOI: 10.1021/BI900075D
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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