5EJZ
Bacterial Cellulose Synthase Product-Bound State
Summary for 5EJZ
| Entry DOI | 10.2210/pdb5ejz/pdb |
| Related | 5EIY 5EJ1 |
| Descriptor | Putative cellulose synthase, UNDECANE, poly(unk), ... (10 entities in total) |
| Functional Keywords | cellulose synthase, translocation, biopolymer, metal binding protein |
| Biological source | Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) More |
| Total number of polymer chains | 3 |
| Total formula weight | 174980.65 |
| Authors | Morgan, J.L.W.,Zimmer, J. (deposition date: 2015-11-02, release date: 2016-03-09, Last modification date: 2023-09-27) |
| Primary citation | Morgan, J.L.,McNamara, J.T.,Fischer, M.,Rich, J.,Chen, H.M.,Withers, S.G.,Zimmer, J. Observing cellulose biosynthesis and membrane translocation in crystallo. Nature, 531:329-334, 2016 Cited by PubMed Abstract: Many biopolymers, including polysaccharides, must be translocated across at least one membrane to reach their site of biological function. Cellulose is a linear glucose polymer synthesized and secreted by a membrane-integrated cellulose synthase. Here, in crystallo enzymology with the catalytically active bacterial cellulose synthase BcsA-BcsB complex reveals structural snapshots of a complete cellulose biosynthesis cycle, from substrate binding to polymer translocation. Substrate- and product-bound structures of BcsA provide the basis for substrate recognition and demonstrate the stepwise elongation of cellulose. Furthermore, the structural snapshots show that BcsA translocates cellulose via a ratcheting mechanism involving a 'finger helix' that contacts the polymer's terminal glucose. Cooperating with BcsA's gating loop, the finger helix moves 'up' and 'down' in response to substrate binding and polymer elongation, respectively, thereby pushing the elongated polymer into BcsA's transmembrane channel. This mechanism is validated experimentally by tethering BcsA's finger helix, which inhibits polymer translocation but not elongation. PubMed: 26958837DOI: 10.1038/nature16966 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.94 Å) |
Structure validation
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