4P02
Structure of Bacterial Cellulose Synthase with cyclic-di-GMP bound.
Summary for 4P02
| Entry DOI | 10.2210/pdb4p02/pdb |
| Related | 4HG6 4P00 |
| Descriptor | Cellulose Synthase subunit A, Cellulose Synthase subunit B, unidentified peptide, ... (8 entities in total) |
| Functional Keywords | membrane protein, allosteric activator, biofilm formation, cellulose biosynthesis, transferase |
| Biological source | Rhodobacter sphaeroides More |
| Total number of polymer chains | 3 |
| Total formula weight | 174854.58 |
| Authors | Morgan, J.L.W.,McNamara, J.T.,Zimmer, J. (deposition date: 2014-02-20, release date: 2014-04-09, Last modification date: 2024-11-06) |
| Primary citation | Morgan, 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: 24704788DOI: 10.1038/nsmb.2803 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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