5GT1
crystal structure of cbpa from L. salivarius REN
Summary for 5GT1
| Entry DOI | 10.2210/pdb5gt1/pdb |
| Descriptor | Choline binding protein A, ZINC ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | s-layer proteins, probiotics, choline-binding protein |
| Biological source | Lactobacillus salivarius str. Ren |
| Total number of polymer chains | 1 |
| Total formula weight | 19132.28 |
| Authors | |
| Primary citation | Wang, R.,Jiang, L.,Zhang, M.,Zhao, L.,Hao, Y.,Guo, H.,Sang, Y.,Zhang, H.,Ren, F. The Adhesion of Lactobacillus salivarius REN to a Human Intestinal Epithelial Cell Line Requires S-layer Proteins Sci Rep, 7:44029-44029, 2017 Cited by PubMed Abstract: Lactobacillus salivarius REN, a novel probiotic isolated from Chinese centenarians, can adhere to intestinal epithelial cells and subsequently colonize the host. We show here that the surface-layer protein choline-binding protein A (CbpA) of L. salivarius REN was involved in adherence to the human colorectal adenocarcinoma cell line HT-29. Adhesion of a cbpA deletion mutant was significantly reduced compared with that of wild-type, suggesting that CbpA acts as an adhesin that mediates the interaction between the bacterium and its host. To identify the molecular mechanism of adhesion, we determined the crystal structure of a truncated form of CbpA that is likely involved in binding to its cell-surface receptor. The crystal structure identified CbpA as a peptidase of the M23 family whose members harbor a zinc-dependent catalytic site. Therefore, we propose that CbpA acts as a multifunctional surface protein that cleaves the host extracellular matrix and participates in adherence. Moreover, we identified enolase as the CbpA receptor on the surface of HT-29 cells. The present study reveals a new class of surface-layer proteins as well as the molecular mechanism that may contribute to the ability of L. salivarius REN to colonize the human gut. PubMed: 28281568DOI: 10.1038/srep44029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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