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SUMMARY:Structure characterization of the Chlamydomonas reinhardtii magnes
 ium chelatase GUN4 and H subunits by small-angle X-ray scattering
DTSTART;VALUE=DATE-TIME:20141120T063000Z
DTEND;VALUE=DATE-TIME:20141120T080000Z
DTSTAMP;VALUE=DATE-TIME:20260815T122220Z
UID:indico-contribution-774@events01.synchrotron.org.au
DESCRIPTION:Speakers: shabnam Tarahi Tabrizi (macquarie university)\nThe m
 agnesium chelatase enzyme catalyses the ATP dependent insertion of Mg+ in 
 to protoporphyrin IX(PPIX) in the first step of the chlorophyll biosynthes
 is pathway consists three different protein subunits ChlI ChlD and ChlH. T
 he GUN4 protein is a regulatory subunit of Mg-chelatase that binds the chl
 orophyll biosynthesis intermediates\, PPIX and Mg protoporphyrin(Mg-PPIX)\
 , stimulates Mg chelatase activity\, and is implicated in developmental si
 gnaling pathway between the chloroplast and nucleus. ChlH is the largest s
 ubunit of Mg-chelatase which also binds both PPIX substrate and the Mg-PPI
 X product. GUN4 appears to participate in a plastid-to-nucleus signalling 
 pathway possibly through regulating Mg-PPIX synthesis or trafficking. Unli
 ke the cyanobacterial GUN4\, the chloroplastic orthologous have an extra C
 -terminal domain that is phosphorylated and is required for magnesium chel
 atase activity. We have determined the low resolution solution structure o
 f GUN4 \, H and the GUN4-H-PPIX complex at ~20 A°\, by using (SAXS) small
 -angle x-ray scattering and can report that the GUN4 protein has a more el
 ongated structure compared to the cyanobacterial protein. Furthermore\, Th
 e SAXS structure of the GUN4-H-PPIX complex is similar to the SAXS structu
 re of H subunit suggesting that GUN4–PPIX may attach somewhere inside th
 e cage shape structure of H subunit to form a complex.\n\nhttps://events01
 .synchrotron.org.au/event/3/contributions/774/
LOCATION: NCSS Exhibition Area
URL:https://events01.synchrotron.org.au/event/3/contributions/774/
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