AI Article Synopsis
- The crystal structure of the trans-acyltransferase (AT) from disorazole polyketide synthase was resolved at 2.5 Å using an innovative sample delivery method with an X-ray free-electron laser.
- A novel sample extractor was employed to efficiently deliver microcrystals from the crystallization solution directly into the X-ray beam at room temperature.
- The observed structure highlighted key catalytic features of the enzyme, including conformational changes around the active site, which are significant for understanding polyketide synthase reaction dynamics.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5721673 | PMC |
| http://dx.doi.org/10.1021/acs.biochem.7b00711 | DOI Listing |
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