2W1K

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

2W1K の概要

• エントリーDOI: 10.2210/pdb2w1k/pdb
• 分子名称: PUTATIVE SORTASE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• 機能のキーワード: pilus, sortase, pneumococcus, pathogenicity, transferase
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57215.20

構造登録者

Manzano, C.,Contreras-Martel, C.,El Mortaji, L.,Izore, T.,Fenel, D.,Vernet, T.,Schoehn, G.,Di Guilmi, A.M.,Dessen, A. (登録日: 2008-10-17, 公開日: 2008-12-23, 最終更新日: 2023-12-13)

主引用文献

Manzano, 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

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

実験手法

X-RAY DIFFRACTION (2.14 Å)