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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.

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.

SUBMITTER: Mathews II 

PROVIDER: S-EPMC5721673 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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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.

Mathews Irimpan I II   Allison Kim K   Robbins Thomas T   Lyubimov Artem Y AY   Uervirojnangkoorn Monarin M   Brunger Axel T AT   Khosla Chaitan C   DeMirci Hasan H   McPhillips Scott E SE   Hollenbeck Michael M   Soltis Michael M   Cohen Aina E AE  

Biochemistry 20170831 36

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  ...[more]

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