Crystal structure of Thermobifida fusca cis-prenyltransferase reveals the dynamic nature of its RXG motif-mediated inter-subunit interactions critical for its catalytic activity-Reference-Cited by-同舟云学术

Crystal structure of Thermobifida fusca cis-prenyltransferase reveals the dynamic nature of its RXG motif-mediated inter-subunit interactions critical for its catalytic activity

Published:2020-11 Issue:3 Volume:532 Page:459-465
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Kurokawa Hirofumi^ORCID,Ambo Takanori,Takahashi Seiji^ORCID,Koyama Tanetoshi

Funder

JSPS KAKENHI

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference23 articles.

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3. Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase;Fujihashi;Proc. Natl. Acad. Sci. U. S. A.,2001

4. The structural basis of chain length control in Rv1086;Wang;J. Mol. Biol.,2008

5. Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases;Shimizu;J. Biol. Chem.,1998

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