Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA

G. Xu, X. Li, P.J. Andrew, Garry Lindsay Taylor

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

Abstract

Streptococcus pneumoniae genomes encode three sialidases, NanA, NanB and NanC, which are key virulence factors that remove sialic acids from various glycoconjugates. The enzymes have potential as drug targets and also as vaccine candidates. The 115 kDa NanA is the largest of the three sialidases and is anchored to the bacterial membrane. Although recombinantly expressed full-length NanA was soluble, it failed to crystallize; therefore, a 56.5 kDa domain that retained full enzyme activity was subcloned. The purified enzyme was crystallized in 0.1 M MES pH 6.5, 30%(w/v) PEG 4000 using the sitting-drop vapour-diffusion method. Data were collected at 100 K to 2.5 angstrom resolution from a crystal grown in the presence of the inhibitor 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 49.2, b = 95.6, c = 226.6 angstrom. The structure was solved by molecular replacement and refined to final R and R-free factors of 0.246 and 0.298, respectively.

Original languageEnglish
Pages (from-to)772-775
Number of pages4
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume64
DOIs
Publication statusPublished - Sept 2008

Keywords

  • TRYPANOSOMA-RANGELI SIALIDASE
  • TRANS-SIALIDASE
  • NEURAMINIDASE
  • SOFTWARE
  • ENZYME

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