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BEGIN:VEVENT
SUMMARY:Welcome and Organisational Update
DTSTART;VALUE=DATE-TIME:20141119T220000Z
DTEND;VALUE=DATE-TIME:20141119T224500Z
DTSTAMP;VALUE=DATE-TIME:20260720T001708Z
UID:indico-contribution-214-728@events01.synchrotron.org.au
DESCRIPTION:Speakers: Andrew Peele ()\, Michael James (Australian Synchrot
 ron)\nhttps://events01.synchrotron.org.au/event/3/contributions/728/
LOCATION: Oliphant Auditorium
URL:https://events01.synchrotron.org.au/event/3/contributions/728/
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BEGIN:VEVENT
SUMMARY:Investigating Molecular Power Converters
DTSTART;VALUE=DATE-TIME:20141119T224500Z
DTEND;VALUE=DATE-TIME:20141119T233000Z
DTSTAMP;VALUE=DATE-TIME:20260720T001708Z
UID:indico-contribution-214-644@events01.synchrotron.org.au
DESCRIPTION:Speakers: Daniela Stock (Victor Chang Cardiac Research Institu
 te)\nRotary ATPases are ubiquitous protein complexes that couple the trans
 location of protons through membranes to the synthesis or hydrolysis of AT
 P and are thus central to biological energy conversion. Eukaryotic F-type 
 ATP synthases use energy stored in transmembrane proton gradients to synth
 esise the biological energy carrier ATP from ADP and inorganic phosphate. 
 The evolutionary related V-type ATPases operate in reverse by utilising en
 ergy derived from ATP hydrolysis to build up transmembrane ion gradients t
 hereby enabling transport processes across membranes. Most eubacteria have
  F-type ATPases\, but some eubacteria and all known archaea have ATPases o
 f the A-type\, which are close homologues of V-ATPases. A-ATPases are simp
 ler in design than their eukaryotic counterparts\, but are bifunctional an
 d can operate in either direction in dependence of their cellular environm
 ent (1). \nWe are using a combination of X-ray structure analysis\, electr
 on microscopy and other biochemical and biophysical techniques to obtain a
  pseudo-atomic model of an A-ATPase (2\, 3). In addition\, X-ray structure
 s in different conformations along with normal mode analysis suggest a gre
 ater dynamics of the intact complex than previously envisioned. This might
  be important for cooperativity and regulation of intact rotary ATPases (4
 \, 5).\n1. Stewart et al. BioArchitecture 3 (2013)\n2. Zhou\, et al. Scien
 ce 334\, 380-385 (2011)\n3. Lee\, et al. Nat. Struct. Mol. Biol. 17\, 373-
 378 (2010)\n4. Stewart\, et al. Nature Communications 3\, 687 (2012)\n5. S
 tewart et al. Current Opinion Structural Biology 25\, 40-48 (2014)\n\nhttp
 s://events01.synchrotron.org.au/event/3/contributions/644/
LOCATION: Oliphant Auditorium
URL:https://events01.synchrotron.org.au/event/3/contributions/644/
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