Summary
PDB 3B97 deposited: 2007-11-02 modified: 2009-02-24
Title Crystal Structure of human Enolase 1
Authors Chung, S.J., Jung, S.K., Kang, H.J., Kim, S.J.
Method X-RAY DIFFRACTION
Structure factors resolution 2.2 rfactor 0.184 rfree 0.217
DPI 0.45 theoretical min: 0.22
Citations

Aside from its enzymatic function in the glycolytic pathway, alpha-enolase (ENO1) has been implicated in numerous diseases, including metastatic cancer, autoimmune disorders, ischaemia and bacterial infection. The disease-related roles of ENO1 are mostly attributed to its immunogenic capacity, DNA-binding ability and plasmin(ogen) receptor function, which are significantly affected by its three-dimensional structure and surface properties, rather than its enzymatic activity. Here, the crystal structure of human ENO1 (hENO1) is presented at 2.2 A resolution. Despite its high sequence similarity to other enolases, the hENO1 structure exhibits distinct surface properties, explaining its various activities, including plasmin(ogen) and DNA binding.

Acta Crystallogr.,Sect.D 2008 Jun; 64(Pt 6):651-657 doi:10.1107/S0907444908008561

Cross References
Database source Identifier Description
PubMed 18560153 ABCRE6
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
3B97/1 3B97 1 dimer 0 2 6 5528
3B97/2 3B97 2 dimer 0 2 6 5450