3ZLF

Structure of group A Streptococcal enolase K312A mutant

3ZLF の概要

• エントリーDOI: 10.2210/pdb3zlf/pdb
• 関連するPDBエントリー: 3ZLG 3ZLH
• 分子名称: ENOLASE, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: lyase, plasminogen-binding
• 由来する生物種: STREPTOCOCCUS PYOGENES MGAS10394
• 細胞内の位置: Cytoplasm : Q5XD01
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 198833.63

構造登録者

Cork, A.J.,Ericsson, D.J.,Law, R.H.P.,Casey, L.W.,Valkov, E.,Bertozzi, C.,Stamp, A.,Aquilina, J.A.,Whisstock, J.C.,Walker, M.J.,Kobe, B. (登録日: 2013-01-31, 公開日: 2014-02-05, 最終更新日: 2023-12-20)

主引用文献

Cork, A.J.,Ericsson, D.J.,Law, R.H.P.,Casey, L.W.,Valkov, E.,Bertozzi, C.,Stamp, A.,Jovcevski, B.,Aquilina, J.A.,Whisstock, J.C.,Walker, M.J.,Kobe, B.
Stability of the Octameric Structure Affects Plasminogen-Binding Capacity of Streptococcal Enolase.
Plos One, 10:21764-, 2015

PubMed Abstract: Group A Streptococcus (GAS) is a human pathogen that has the potential to cause invasive disease by binding and activating human plasmin(ogen). Streptococcal surface enolase (SEN) is an octameric α-enolase that is localized at the GAS cell surface. In addition to its glycolytic role inside the cell, SEN functions as a receptor for plasmin(ogen) on the bacterial surface, but the understanding of the molecular basis of plasmin(ogen) binding is limited. In this study, we determined the crystal and solution structures of GAS SEN and characterized the increased plasminogen binding by two SEN mutants. The plasminogen binding ability of SENK312A and SENK362A is ~2- and ~3.4-fold greater than for the wild-type protein. A combination of thermal stability assays, native mass spectrometry and X-ray crystallography approaches shows that increased plasminogen binding ability correlates with decreased stability of the octamer. We propose that decreased stability of the octameric structure facilitates the access of plasmin(ogen) to its binding sites, leading to more efficient plasmin(ogen) binding and activation.

PubMed: 25807546
DOI: 10.1371/JOURNAL.PONE.0121764

実験手法

X-RAY DIFFRACTION (2.15 Å)