3ZLG

Structure of group A Streptococcal enolase K362A mutant

Summary for 3ZLG

• Entry DOI: 10.2210/pdb3zlg/pdb
• Related: 3ZLF 3ZLH
• Descriptor: ENOLASE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: lyase, plasminogen-binding
• Biological source: STREPTOCOCCUS PYOGENES MGAS10394
• Cellular location: Cytoplasm : Q5XD01
• Total number of polymer chains: 4
• Total formula weight: 198833.63

Authors

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. (deposition date: 2013-01-31, release date: 2014-02-05, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)