Crystal Structure of Spy0129, a Streptococcus pyogenes Class B Sortase Involved in Pilus Assembly

Kang, Hae Joo; Coulibaly, Fasséli; Proft, Thomas; Baker, Edward N.

doi:10.1371/journal.pone.0015969

Title: Crystal Structure of Spy0129, a Streptococcus pyogenes Class B Sortase Involved in Pilus Assembly

Journal Article · Tue Jan 11 00:00:00 EST 2011 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0015969· OSTI ID:1627442

Kang, Hae Joo ^[1]; Coulibaly, Fasséli ^[1]; Proft, Thomas ^[2]; Baker, Edward N. ^[1]

Univ. of Auckland (New Zealand). Maurice Wilkins Centre for Molecular Biodiscovery; Univ. of Auckland (New Zealand). School of Biological Sciences
Univ. of Auckland (New Zealand). Maurice Wilkins Centre for Molecular Biodiscovery; Univ. of Auckland (New Zealand). School of Medical Sciences

Sortase enzymes are cysteine transpeptidases that mediate the covalent attachment of substrate proteins to the cell walls of Gram-positive bacteria, and thereby play a crucial role in virulence, infection and colonisation by pathogens. Many cellsurface proteins are anchored by the housekeeping sortase SrtA but other more specialised sortases exist that attach subsets of proteins or function in pilus assembly. The sortase Spy0129, or SrtC1, from the M1 SF370 strain of Streptococcus pyogenes is responsible for generating the covalent linkages between the pilin subunits in the pili of this organism. The crystal structure of Spy0129 has been determined at 2.3 Å resolution (R = 20.4%, Rfree = 26.0%). The structure shows that Spy0129 is a class B sortase, in contrast to other characterised pilin polymerases, which belong to class C. Spy0129 lacks a flap believed to function in substrate recognition in class C enzymes and instead has an elaborated β6/β7 loop. The two independent Spy0129 molecules in the crystal show differences in the positions and orientations of the catalytic Cys and His residues, Cys221 and His126, correlated with movements of the β7/β8 and β4/β5 loops that respectively follow these residues. Bound zinc ions stabilise these alternative conformations in the crystal. This conformational variability is likely to be important for function although there is no evidence that zinc is involved in vivo.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); Health Research Council of New Zealand; Foundation for Research, Science and Technology of New Zealand; USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1627442

Journal Information:: PLoS ONE, Vol. 6, Issue 1; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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