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2W1K

Crystal Structure of Sortase C-3 (SRTC-3) from Streptococcus pneumoniae

Summary for 2W1K
Entry DOI10.2210/pdb2w1k/pdb
DescriptorPUTATIVE SORTASE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
Functional Keywordspilus, sortase, pneumococcus, pathogenicity, transferase
Biological sourceSTREPTOCOCCUS PNEUMONIAE
Total number of polymer chains2
Total formula weight57215.20
Authors
Manzano, C.,Contreras-Martel, C.,El Mortaji, L.,Izore, T.,Fenel, D.,Vernet, T.,Schoehn, G.,Di Guilmi, A.M.,Dessen, A. (deposition date: 2008-10-17, release date: 2008-12-23, Last modification date: 2023-12-13)
Primary citationManzano, C.,Contreras-Martel, C.,El Mortaji, L.,Izore, T.,Fenel, D.,Vernet, T.,Schoehn, G.,Di Guilmi, A.M.,Dessen, A.
Sortase-Mediated Pilus Fiber Biogenesis in Streptococcus Pneumoniae.
Structure, 16:1838-, 2008
Cited by
PubMed Abstract: Streptococcus pneumoniae is a piliated pathogen whose ability to circumvent vaccination and antibiotic treatment strategies is a cause of mortality worldwide. Pili play important roles in pneumococcal infection, but little is known about their biogenesis mechanism or the relationship between components of the pilus-forming machinery, which includes the fiber pilin (RrgB), two minor pilins (RrgA, RrgC), and three sortases (SrtC-1, SrtC-2, SrtC-3). Here we show that SrtC-1 is the main pilus-polymerizing transpeptidase, and electron microscopy analyses of RrgB fibers reconstituted in vitro reveal that they structurally mimic the pneumococcal pilus backbone. Crystal structures of both SrtC-1 and SrtC-3 reveal active sites whose access is controlled by flexible lids, unlike in non-pilus sortases, and suggest that substrate specificity is dictated by surface recognition coupled to lid opening. The distinct structural features of pilus-forming sortases suggest a common pilus biogenesis mechanism that could be exploited for the development of broad-spectrum antibacterials.
PubMed: 19081060
DOI: 10.1016/J.STR.2008.10.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.14 Å)
Structure validation

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数据于2024-10-30公开中

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