6APF
Trans-acting transferase from Disorazole synthase complexed with Citrate.
Summary for 6APF
| Entry DOI | 10.2210/pdb6apf/pdb |
| Descriptor | DisD protein, CITRIC ACID, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | acyl transferase, disorazole synthase, citrate complex, polyketide synthase, transferase |
| Biological source | Sorangium cellulosum |
| Total number of polymer chains | 2 |
| Total formula weight | 62198.76 |
| Authors | Mathews, I.I.,Lyubimov, A.,Soltis, M.,Khosla, C.,Cohen, A.,Robbins, T. (deposition date: 2017-08-17, release date: 2018-04-04, Last modification date: 2023-10-04) |
| Primary citation | Mathews, I.I.,Allison, K.,Robbins, T.,Lyubimov, A.Y.,Uervirojnangkoorn, M.,Brunger, A.T.,Khosla, C.,DeMirci, H.,McPhillips, S.E.,Hollenbeck, M.,Soltis, M.,Cohen, A.E. The Conformational Flexibility of the Acyltransferase from the Disorazole Polyketide Synthase Is Revealed by an X-ray Free-Electron Laser Using a Room-Temperature Sample Delivery Method for Serial Crystallography. Biochemistry, 56:4751-4756, 2017 Cited by PubMed Abstract: The crystal structure of the trans-acyltransferase (AT) from the disorazole polyketide synthase (PKS) was determined at room temperature to a resolution of 2.5 Å using a new method for the direct delivery of the sample into an X-ray free-electron laser. A novel sample extractor efficiently delivered limited quantities of microcrystals directly from the native crystallization solution into the X-ray beam at room temperature. The AT structure revealed important catalytic features of this core PKS enzyme, including the occurrence of conformational changes around the active site. The implications of these conformational changes for polyketide synthase reaction dynamics are discussed. PubMed: 28832129DOI: 10.1021/acs.biochem.7b00711 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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