Structural highlights
6tzk is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[BCSC_ECOLI] Required for maximal bacterial cellulose synthesis.
Publication Abstract from PubMed
Extracellular bacterial cellulose contributes to biofilm stability and to the integrity of the bacterial cell envelope. In Gram-negative bacteria, cellulose is synthesized and secreted by a multi-component cellulose synthase complex. The BcsA subunit synthesizes cellulose and also transports the polymer across the inner membrane. Translocation across the outer membrane occurs through the BcsC porin, which extends into the periplasm via 19 tetra-tricopeptide repeats (TPR). We present the crystal structure of a truncated BcsC, encompassing the last TPR repeat and the complete outer membrane channel domain, revealing a 16-stranded, beta barrel pore architecture. The pore is blocked by an extracellular gating loop, while the extended C terminus inserts deeply into the channel and positions a conserved Trp residue near its extracellular exit. The channel is lined with hydrophilic and aromatic residues suggesting a mechanism for facilitated cellulose diffusion based on aromatic stacking and hydrogen bonding.
Architecture of the Cellulose Synthase Outer Membrane Channel and Its Association with the Periplasmic TPR Domain.,Acheson JF, Derewenda ZS, Zimmer J Structure. 2019 Oct 1. pii: S0969-2126(19)30314-4. doi:, 10.1016/j.str.2019.09.008. PMID:31604608[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Acheson JF, Derewenda ZS, Zimmer J. Architecture of the Cellulose Synthase Outer Membrane Channel and Its Association with the Periplasmic TPR Domain. Structure. 2019 Oct 1. pii: S0969-2126(19)30314-4. doi:, 10.1016/j.str.2019.09.008. PMID:31604608 doi:http://dx.doi.org/10.1016/j.str.2019.09.008
