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SUMMARY:X-ray structure of a transmembrane domain from an ABC-transporter 
 dependent system from Neisseria meningitidis in a non-biological state
DTSTART;VALUE=DATE-TIME:20211125T073700Z
DTEND;VALUE=DATE-TIME:20211125T073800Z
DTSTAMP;VALUE=DATE-TIME:20260718T063216Z
UID:indico-contribution-4200@events01.synchrotron.org.au
DESCRIPTION:Speakers: Lorelei Masselot--Joubert (University of Western Aus
 tralia)\nMolecular replacement (MR) is the most commonly used method in cr
 ystallography to solve the phase problem required to obtain the three dime
 nsional structure of a protein. Traditionally MR uses a search model from 
 a previously determined protein structure. One of the requirements for suc
 cess by MR is that the amino acid sequences of the search model and the un
 known structure should be have at least 35 % identity. When this is not po
 ssible\, an *ab initio* model can be generated using the sequence of the u
 nsolved protein. In this project\, we used the algorithm\, tr-Rosetta\, fr
 om the Rosetta server to obtain *ab initio* models used for use in MR.\nCt
 rC is part of an ABC transporter dependent complex in *Neisseria meningiti
 s*\, important for capsule polysaccharide transport. It constitutes the tr
 ansmembrane domain and associates with a separate nucleotide binding domai
 n\, CtrD\, making a heterotetramer.  CtrC\, has been crystallised using th
 e lipidic cubic phase (LCP) method. After data collection using the MX2 be
 amline at the Australian Synchrotron\, the structure has been solved at 2.
 87 Å by MR using an *ab initio* derived search model. \nThe structure of 
 CtrC shows a monomeric arrangement in the crystal lattice\, unusual for an
  ABC transporter.  A single molecule of the monoolein lipid used in the LC
 P matrix was found bound within the protein structure.  We hypothesize tha
 t the presence of the monoolein ligand\, and possibly the absence of CtrD\
 , abrogates the ability of CtrC to form the expected dimeric structure.\n\
 nhttps://events01.synchrotron.org.au/event/146/contributions/4200/
LOCATION:Online
URL:https://events01.synchrotron.org.au/event/146/contributions/4200/
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