Title

Homology modeling of Mycoplasma pneumoniae enolase and its molecular interaction with human- plasminogen

Authors

Vasunun Chumchua^{1, 2}, Natapol Pornputtapong^{1, 2}, Chinae Thammarongtham^3, * and Duangdeun Meksuriyen^{1, 4}

Affiliation

¹Department of Biochemistry, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok 10330, Thailand; ²PDTI, King Mongkut’s University of Technology Thonburi (Bangkhuntien), Bangkok, 10150, Thailand; ³Biochemical Engineering and Pilot Plant Research and Development Unit, National Center for Genetic Engineering and Biotechnology, Bangkok, Thailand; ⁴Chulalongkorn University Drug and Health Products Innovation and Promotion Center, Bangkok 10330, Thailand

Email

662 470 7392

662 452 3455; * Corresponding author

Article Type

Hypothesis

Date

received July 31, 2008; accepted August 31, 2008; published September 08, 2008

Abstract

Alpha (α)-enolase (e), a glycolytic enzyme, has an alternative role as a surface receptor of several bacteria mediating plasminogen (pg) binding. It is also recognized as a virulence factor of some pathogenic bacteria facilitating plasminogen activation and host cell invasion. A mycoplasmal α-enolase is also plasminogen binding protein. Molecular interaction of Mycoplasma. pneumoniae enolase with plasminogen would be useful for exploring the pathogen-host interaction. In an attempt to identify plasminogen binding sites of M. pneumoniae enolase, homology modeling and docking studies were conducted to obtain modeled structures of the M. pneumoniae enolase-plasminogen complex. The refined model was validated further by standard methods. Molecular docking revealed hydrogen bonding of eLys70-pgTyr50, eAsn165-pgThr66, eAla168-pgGlu21, eAsp17-pgLys70, and eAsn213-pgPro68/pgAsn69. Substantial decreases in accessible surface area (ASA) were observed and in concurrence with hydrogen bond pattern. These findings provide a detailed prediction of key residues that interact at the protein-protein interface. Our theoretical prediction is consistent with known biochemical data. The predicted interaction complex can be of great assistance in understanding structural insights, which is necessary to pathogen and host-component interaction. The ability of M. pneumoniae enolase to bind plasminogen may be indicative of an important role in invasion of this pathogen to host.

Keywords

Mycoplasma pneumoniae enolase; human plasminogen; homology modeling; molecular docking

Citation

Chumchua et al., Bioinformation 3(1): 18-23 (2008)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics Publishing Group

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.