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DTSTAMP:20260405T161914Z
UID:5b8e591aec68b902188248@ist.ac.at
DTSTART:20180906T140000
DTEND:20180906T150000
DESCRIPTION:Speaker: Prof. Paul Schanda\nhosted by Leonid Sazanov\nAbstract
 : Integrated structure/dynamics/function studies of large protein complexe
 s by NMR &co: from the structural basis of membrane-protein import into mi
 tochondria to dynamic mechanisms of a 0.5 MDa enzymeIntegrated structure/d
 ynamics/function studies of large protein complexes by NMR & co: from the 
 structural basis of membrane-protein import into mitochondria to dynamic m
 echanisms of a 0.5 MDa enzymeProteins are highly dynamic entities. Process
 es such as enzymatic turnover or chaperoning are intimately linked to thei
 r ability to sample multiple conformations. Such complex problems are best
  tackled by an integrated approach\, combining NMR spectroscopy - which gi
 ves direct access to dynamics with crystal structures\, MD simulations\, S
 AXS and other biophysical methods.In my presentation I will highlight two 
 recent examples of integrated structural biology approaches from my group.
 The first part will focus on an important biological question of mitochond
 rial biogenesis: how are the highly aggregation-prone membrane proteins\, 
 synthesized far from their final destination\, transported to their respec
 tive membranes? We will show the structural basis of the mode of action of
  the mitochondrial chaperone TIM910\, while it carries mitochondrial membr
 ane proteins. Our NMR/MD/SAXS/in-vivo approach reveals a highly dynamic ch
 aperone machinery and provides a rationale for dysfunction and disease rel
 ated to this chaperone system.In the second part I will present our recent
  results on the 0.5 MDa-large aminopeptidase enzyme machinery TET2. We sho
 w how one can combine medium-resolution EM data with NMR data to obtain a 
 high-resolution structure de novo. Furthermore\, we reveal how dynamic par
 ts of the protein are at the heart of enzymatic function -- including part
 s that are even missing in crystal structures\, and how NMR deciphers deta
 ils of substrate traficking and active-site binding.Taken together\, I wil
 l provide an overview ranging from methodological advances\, including the
  integrated use of multiple structural/biological techniques\, to challeng
 ing biological questions and how structural biology can resolve mechanisti
 c questions.
LOCATION:Mondi Seminar Room 2\, Central Building\, ISTA
ORGANIZER:rsix@ist.ac.at
SUMMARY:Prof. Paul Schanda: Integrated structure/dynamics/function studies 
 of large protein complexes by NMR
URL:https://talks-calendar.ista.ac.at/events/1389
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