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SUMMARY:Short Talk 11\, Raminta Venskutonytè - UrdA: structural character
 ization of a novel enzyme
DTSTART;VALUE=DATE-TIME:20191011T080000Z
DTEND;VALUE=DATE-TIME:20191011T082000Z
DTSTAMP;VALUE=DATE-TIME:20260526T060938Z
UID:indico-contribution-772@lindico453.srv.lu.se
DESCRIPTION:Speakers: Raminta Venskutonytė (Medical Structural Biology\, 
 Lund University)\nUrocanate reductase (UrdA) is a bacterial enzyme that wa
 s first characterized in\n2012 and shown to reduce urocanic acid resulting
  in a product imidazole propionate\n(1). Unlike similar enzymes fumarate r
 eductases\, UrdA hasn’t been well investigated.\nBesides being an intere
 sting novel enzyme enabling bacteria to grow in anaerobic\nconditions with
  urocanic acid as electron acceptor (1)\, UrdA was shown to play a\nsignif
 icant role in human gut microbiota\, as imidazole propionate levels are\ni
 ncreased in people with type 2 diabetes and it further affects glucose met
 abolism\n(2).\nTwo domain construct of UrdA\, consisting of a FAD binding 
 and a mobile domain\nwere successfully expressed\, purified and crystalliz
 ed. Four X-ray structures were\nobtained depicting different states of the
  enzyme: ADP bound\, FAD bound\,\nsubstrate/FAD bound and in complex with 
 product/FAD. The data reveals the overall\nstructural arrangement of the e
 nzyme as well as the substrate binding mode and\nconformational changes.\n
 The role of UrdA in imidazole propionate production in relation to type 2 
 diabetes\nmakes the first structure of the UrdA of particular importance t
 o our understanding of\nthis enzyme.\n\nReferences\n1. Bogachev\, A. V. et
  al. (2012)\, Urocanate reductase of Shewanella. Molecular\nMicrobiology\,
  86: 1452-1463.\n2. Koh A. et al. (2018) Microbially Produced Imidazole Pr
 opionate Impairs Insulin\nSignaling through mTORC1. Cell 175: 947-961.\n\n
 https://lindico453.srv.lu.se/event/125/contributions/772/
LOCATION:Kulturen Auditorium
URL:https://lindico453.srv.lu.se/event/125/contributions/772/
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