8HKB
TPA bound-form of Periplasmic terephthalate binding protein (TBP) from Ideonella sakaiensis mutant K184D
Summary for 8HKB
| Entry DOI | 10.2210/pdb8hkb/pdb |
| Descriptor | Periplasmic terephthalate binding protein (TBP), terephthalic acid (3 entities in total) |
| Functional Keywords | periplasmic protein, terephthalate binding protein, transportation protein, ideonella sakaiensis, transport protein |
| Biological source | Ideonella sakaiensis |
| Total number of polymer chains | 1 |
| Total formula weight | 32870.32 |
| Authors | Lee, S.H.,Seo, H.,Kim, K.-J. (deposition date: 2022-11-25, release date: 2023-06-21, Last modification date: 2024-05-22) |
| Primary citation | Lee, S.H.,Seo, H.,Hong, H.,Kim, M.,Kim, K.J. Molecular mechanism underlying high-affinity terephthalate binding and conformational change of TBP from Ideonella sakaiensis. Int.J.Biol.Macromol., 243:125252-125252, 2023 Cited by PubMed Abstract: Ideonella sakaiensis is the bacterium that can survive by degrading polyethylene terephthalate (PET) plastic, and terephthalic acid (TPA) binding protein (IsTBP) is an essential periplasmic protein for uptake of TPA into the cytosol for complete degradation of PET. Here, we demonstrated that IsTBP has remarkably high specificity for TPA among 33 monophenolic compounds and two 1,6-dicarboxylic acids tested. Structural comparisons with 6-carboxylic acid binding protein (RpAdpC) and TBP from Comamonas sp. E6 (CsTphC) revealed the key structural features that contribute to high TPA specificity and affinity of IsTBP. We also elucidated the molecular mechanism underlying the conformational change upon TPA binding. In addition, we developed the IsTBP variant with enhanced TPA sensitivity, which can be expanded for the use of TBP as a biosensor for PET degradation. PubMed: 37295700DOI: 10.1016/j.ijbiomac.2023.125252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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