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SUMMARY:Understanding the interaction between the Proteus mirabilis Scs pr
 oteins using neutron scattering
DTSTART;VALUE=DATE-TIME:20181120T003000Z
DTEND;VALUE=DATE-TIME:20181120T005000Z
DTSTAMP;VALUE=DATE-TIME:20260813T174841Z
UID:indico-contribution-2348@events01.synchrotron.org.au
DESCRIPTION:Speakers: Andrew Whitten (ANSTO)\nCorrectly forming disulphide
  bonds is critical to the folding of a wide variety of proteins. Bacterial
  virulence factors are one class of proteins containing disulfide bonds\, 
 thus\, an approach to disarm virulent bacterial might involve shutting dow
 n the machinery involved in the formation of disulfide bonds. The suppress
 or of copper sensitivity (Scs) proteins form part of the disulfide bond fo
 rming machinery in bacteria\, and it is hoped that determining the structu
 re of molecules such as this may lead to the development of new classes of
  antibiotics. There are four Scs proteins (ScsA\, B\, C and D) present in 
 numerous Gram-negative bacteria\, and few have been structurally character
 ised. In this work\, we have created cysteine variants of PmScsC and PmScs
 B to produce a stable complex and using small-angle X-ray and neutron scat
 tering with contrast variation\, we have determined the low-resolution str
 ucture of the PmScsC–PmScsB complex.\n\nhttps://events01.synchrotron.org
 .au/event/84/contributions/2348/
LOCATION:AINSE Conference Centre New Illawarra Road Lucas Heights NSW 2234
  Australia
URL:https://events01.synchrotron.org.au/event/84/contributions/2348/
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