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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cueno, Marni E. Nagano, Keiji Imai, Kenichi Tamura, Muneaki Yoshimura, Fuminobu Ochiai, Kuniyasu |
| Description | Author Affiliation: Cueno ME ( Department of Microbiology, Nihon University, School of Dentistry, Tokyo 101-8310, Japan. Electronic address: marni.cueno@nihon-u.ac.jp.); Nagano K ( Department of Microbiology, School of Dentistry, Aichi Gakuin University, Nagoya 464-8650, Japan.); Imai K ( Department of Microbiology, Nihon University, School of Dentistry, Tokyo 101-8310, Japan.); Tamura M ( Department of Microbiology, Nihon University, School of Dentistry, Tokyo 101-8310, Japan.); Yoshimura F ( Department of Microbiology, School of Dentistry, Aichi Gakuin University, Nagoya 464-8650, Japan.); Ochiai K ( Department of Microbiology, Nihon University, School of Dentistry, Tokyo 101-8310, Japan. Electronic address: ochiai.kuniyasu@nihon-u.ac.jp.) |
| Abstract | Porphyromonas gingivalis FimA is a major aetiological agent in periodontal disease development, however, its structure has never been determined. Here, we established the mature P. gingivalis FimA ab initio model of all six FimA variants. We determined the conserved amino acid sequences of each FimA variant and generated mature FimA models. Subsequently, we validated their quality, protein empirical distribution, and radius of gyration. Similarly, structural comparison and topological orientation were elucidated, and the probable protein-protein docking was investigated. We found that the putative mature FimA model is ß-sheet-rich and, likewise, we observed that each mature FimA model has varying levels of structural differences which can be topologically subdivided into the upper, middle, and lower FimA sections. Moreover, we found that the FimA epithelial cell-binding domain (EBD) is structurally conserved within the middle FimA section of all variants and FimA-FimA docking suggests that the FimA EBDs are oriented in opposite and alternating directions of each other. |
| File Format | HTM / HTML |
| ISSN | 10933263 |
| Journal | Journal of Molecular Graphics and Modelling |
| Volume Number | 55 |
| e-ISSN | 18734243 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-02-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Molecular Biology Bacterial Proteins Chemistry Molecular Docking Simulation Porphyromonas Gingivalis Epithelial Cells Metabolism Protein Structure, Secondary Protein Structure, Tertiary Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Computer Graphics and Computer-Aided Design Spectroscopy Materials Chemistry Physical and Theoretical Chemistry |
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