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4P02

Structure of Bacterial Cellulose Synthase with cyclic-di-GMP bound.

Summary for 4P02
Entry DOI10.2210/pdb4p02/pdb
Related4HG6 4P00
DescriptorCellulose Synthase subunit A, Cellulose Synthase subunit B, unidentified peptide, ... (8 entities in total)
Functional Keywordsmembrane protein, allosteric activator, biofilm formation, cellulose biosynthesis, transferase
Biological sourceRhodobacter sphaeroides
More
Total number of polymer chains3
Total formula weight174854.58
Authors
Morgan, J.L.W.,McNamara, J.T.,Zimmer, J. (deposition date: 2014-02-20, release date: 2014-04-09, Last modification date: 2023-12-27)
Primary citationMorgan, J.L.,McNamara, J.T.,Zimmer, J.
Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP.
Nat.Struct.Mol.Biol., 21:489-496, 2014
Cited by
PubMed Abstract: 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.
PubMed: 24704788
DOI: 10.1038/nsmb.2803
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

226707

數據於2024-10-30公開中

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