title: Structure of the stationary phase survival protein YuiC from B.subtilis.
abstract: BACKGROUND
  Stationary phase survival proteins (Sps) were found in Firmicutes as having analogous domain compositions, and in some cases genome context, as the resuscitation promoting factors of Actinobacteria, but with a different putative peptidoglycan cleaving domain.
  
  
  RESULTS
  The first structure of a Firmicute Sps protein YuiC from B. subtilis, is found to be a stripped down version of the cell-wall peptidoglycan hydrolase MltA. The YuiC structures are of a domain swapped dimer, although some monomer is also found in solution. The protein crystallised in the presence of pentasaccharide shows a 1,6-anhydrodisaccharide sugar product, indicating that YuiC cleaves the sugar backbone to form an anhydro product at least on lengthy incubation during crystallisation.
  
  
  CONCLUSIONS
  The structural simplification of MltA in Sps proteins is analogous to that of the resuscitation promoting factor domains of Actinobacteria, which are stripped down versions of lysozyme and soluble lytic transglycosylase proteins.
authors.affiliation: Institute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. d.quay@mail.cryst.bbk.ac.uk.
authors.forename: Doris H X
authors.initials: DH
authors.lastname: Quay
authors.affiliation: Institute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. a.cole@mail.cryst.bbk.ac.uk.
authors.forename: Ambrose R
authors.initials: AR
authors.lastname: Cole
authors.affiliation: Institute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London, WC1E 6BT, UK. a.cryar@ucl.ac.uk.
authors.forename: Adam
authors.initials: A
authors.lastname: Cryar
authors.affiliation: Institute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. k.thalassinos@ucl.ac.uk.|Institute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London, WC1E 6BT, UK. k.thalassinos@ucl.ac.uk.
authors.forename: Konstantinos
authors.initials: K
authors.lastname: Thalassinos
authors.affiliation: Institute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. m.williams@mail.cryst.bbk.ac.uk.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Williams
authors.affiliation: Institute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. s.bhakta@bbk.ac.uk.
authors.forename: Sanjib
authors.initials: S
authors.lastname: Bhakta
authors.affiliation: Institute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. n.keep@mail.cryst.bbk.ac.uk.
authors.forename: Nicholas H
authors.initials: NH
authors.lastname: Keep
mesh_terms: D000135:Acid Phosphatase / Q000737:chemistry*; D001412:Bacillus subtilis / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D016695:Glycosyltransferases / Q000737:chemistry; D008958:Models, Molecular; D009844:Oligosaccharides / Q000378:metabolism; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D009844:Oligosaccharides; D016695:Glycosyltransferases; C085441:MltA protein, bacteria; D000135:Acid Phosphatase