Crystal Structure of the Acid Induced Arginine Decarboxylase from Escherichia coli: Reversible Decamer Assembly Controls Enzyme Activity

DOI: 10.1139/O09-182
PMID: 20453931

Authors: Juni Andrell (Imperial College London) , Matthew Hicks (University of East Anglia) , Tracy Palmer (University of East Anglia) , Liz Carpenter (Imperial college London) , So Iwata (Diamond Light Source) , Megan Maher (Centenary Institute of Cancer Medicine Cell Biology Sydney Australia)
Co-authored by industrial partner: No

Type: Conference Paper

Peer Reviewed: No

State: Published (Approved)
Published: March 2009
Diamond Proposal Number(s): 316

Abstract: Enteric bacteria such as Escherichia coli have acquired a wide array of acid stress response systems to counteract the extreme acidity encountered when invading the host's digestive or urinary tracts. These acid stress response systems are both enzyme and chaperone based. The 3 main enzyme-based acid resistance pathways are glutamate-, arginine-, and lysine-decarboxylase pathways. They are under a complex regulatory network allowing the bacteria to fine tune its response to the external environment. HdeA and HdeB are the main chaperones involved in acid stress response. The decarboxylase systems are also found in Vibrio cholera, Vibrio vulnifus, Shigella flexneri. and Salmonella typhimurium, although some differences exist in their functional mechanism and regulation.

Journal Keywords: Membrane Protein Laboratory

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
Technical Areas: