Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 21, Issue 5, Pages 489-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2803
Keywords
-
Funding
- US Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357, W-31-109-Eng-38]
- US National Cancer Institute [Y1-CO-1020]
- National Institute of General Medical Sciences [Y1-GM-1104]
- US National Science Foundation Graduate Research Fellowship [DGE-1315231]
- US National Institutes of Health grant [R01GM101001]
Ask authors/readers for more resources
The bacterial signaling molecule cyclic di-GMP (c-di-GMP) stimulates the synthesis of bacterial cellulose, which is frequently found in biofilms. Bacterial cellulose is synthesized and translocated across the inner membrane by a complex of cellulose synthase BcsA and BcsB subunits. Here we present crystal structures of the c-di-GMP activated BcsA BcsB complex. The structures reveal that c-di-GMP releases an autoinhibited state of the enzyme by breaking a salt bridge that otherwise tethers a conserved gating loop that controls access to and substrate coordination at the active site. Disrupting the salt bridge by mutagenesis generates a constitutively active cellulose synthase. Additionally, the c-di-GMP activated BcsA BcsB complex contains a nascent cellulose polymer whose terminal glucose unit rests at a new location above BcsA's active site and is positioned for catalysis. Our mechanistic insights indicate how c-di-GMP allosterically modulates enzymatic functions.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available