| Title: | Operating mechanism and molecular dynamics of pheromone-binding protein ASP1 as influenced by pH |
| Author(s): | Han L; Zhang YJ; Zhang L; Cui X; Yu J; Zhang Z; Liu MS; |
| Address: | "Centre for Cancer Molecular Diagnosis, Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center for Cancer, Tianjin, China; State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China. Key Lab for Biological Control of the Ministry of Agriculture, China Agricultural University, Beijing, China. Beijing Computing Center, Beijing, China. Centre for Cancer Molecular Diagnosis, Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center for Cancer, Tianjin, China. State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China. CSIRO - Computational Informatics & Digital Productivity Flagship, Private Bag 10, Clayton South, Australia" |
| DOI: | 10.1371/journal.pone.0110565 |
| ISSN/ISBN: | 1932-6203 (Electronic) 1932-6203 (Linking) |
| Abstract: | "Odorant binding protein (OBP) is a vital component of the olfactory sensation system. It performs the specific role of ferrying odorant molecules to odorant receptors. OBP helps insects and types of animal to sense and transport stimuli molecules. However, the molecular details about how OBPs bind or release its odorant ligands are unclear. For some OBPs, the systems' pH level is reported to impact on the ligands' binding or unbinding capability. In this work we investigated the operating mechanism and molecular dynamics in bee antennal pheromone-binding protein ASP1 under varying pH conditions. We found that conformational flexibility is the key factor for regulating the interaction of ASP1 and its ligands, and the odorant binds to ASP1 at low pH conditions. Dynamics, once triggered by pH changes, play the key roles in coupling the global conformational changes with the odorant release. In ASP1, the C-terminus, the N-terminus, helix alpha2 and the region ranging from helices alpha4 to alpha5 form a cavity with a novel 'entrance' of binding. These are the major regions that respond to pH change and regulate the ligand release. Clearly there are processes of dynamics and hydrogen bond network propagation in ASP1 in response to pH stimuli. These findings lead to an understanding of the mechanism and dynamics of odorant-OBP interaction in OBP, and will benefit chemsensory-related biotech and agriculture research and development" |
| Keywords: | "Animals Bees Carrier Proteins/*chemistry Hydrogen Bonding Hydrogen-Ion Concentration Insect Proteins/*chemistry Molecular Docking Simulation Molecular Dynamics Simulation Pheromones/chemistry Protein Binding Protein Structure, Secondary Protein Structure, ;" |
| Notes: | "MedlineHan, Lei Zhang, Yong-Jun Zhang, Long Cui, Xu Yu, Jinpu Zhang, Ziding Liu, Ming S eng Research Support, Non-U.S. Gov't 2014/10/23 PLoS One. 2014 Oct 22; 9(10):e110565. doi: 10.1371/journal.pone.0110565. eCollection 2014" |
