Structural highlights
4p02 is a 3 chain structure with sequence from Rhos4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| NonStd Res: | |
| Related: | 4hg6, 4p00 |
| Gene: | RSP_0333 (RHOS4), RSP_0332 (RHOS4) |
| Activity: | Cellulose synthase (UDP-forming), with EC number 2.4.1.12 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
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.
Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP.,Morgan JL, McNamara JT, Zimmer J Nat Struct Mol Biol. 2014 Apr 6. doi: 10.1038/nsmb.2803. PMID:24704788[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Morgan JL, McNamara JT, Zimmer J. Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP. Nat Struct Mol Biol. 2014 Apr 6. doi: 10.1038/nsmb.2803. PMID:24704788 doi:http://dx.doi.org/10.1038/nsmb.2803
