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2016 ; 531
(7594
): 329-34
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Observing cellulose biosynthesis and membrane translocation in crystallo
#MMPMID26958837
Morgan JL
; McNamara JT
; Fischer M
; Rich J
; Chen HM
; Withers SG
; Zimmer J
Nature
2016[Mar]; 531
(7594
): 329-34
PMID26958837
show ga
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.