2W20

Structure of the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae

2W20 の概要

• エントリーDOI: 10.2210/pdb2w20/pdb
• 分子名称: SIALIDASE A, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: secreted, cell wall, hydrolase, sialidase, glycosidase, neuraminidase, peptidoglycan-anchor
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): P62576
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106667.57

構造登録者

Xu, G.,Andrew, P.W.,Taylor, G.L. (登録日: 2008-10-21, 公開日: 2008-12-23, 最終更新日: 2024-05-08)

主引用文献

Xu, G.,Li, X.,Andrew, P.W.,Taylor, G.L.
Structure of the Catalytic Domain of Streptococcus Pneumoniae Sialidase Nana.
Acta Crystallogr.,Sect.F, 64:772-, 2008

PubMed 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 A 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 A. The structure was solved by molecular replacement and refined to final R and R(free) factors of 0.246 and 0.298, respectively.

PubMed: 18765901
DOI: 10.1107/S1744309108024044

実験手法

X-RAY DIFFRACTION (1.49 Å)