Abstract:
:The cellulose synthesizing terminal complex consisting of subunits A, B, C, and D in Acetobacter xylinum spans the outer and inner cell membranes to synthesize and extrude glucan chains, which are assembled into subelementary fibrils and further into a ribbon. We determined the structures of subunit D (AxCeSD/AxBcsD) with both N- and C-terminal His(6) tags, and in complex with cellopentaose. The structure of AxCeSD shows an exquisite cylinder shape (height: ∼65 Å, outer diameter: ∼90 Å, and inner diameter: ∼25 Å) with a right-hand twisted dimer interface on the cylinder wall, formed by octamer as a functional unit. All N termini of the octamer are positioned inside the AxCeSD cylinder and create four passageways. The location of cellopentaoses in the complex structure suggests that four glucan chains are extruded individually through their own passageway along the dimer interface in a twisted manner. The complex structure also shows that the N-terminal loop, especially residue Lys6, seems to be important for cellulose production, as confirmed by in vivo assay using mutant cells with axcesD gene disruption and N-terminus truncation. Taking all results together, a model of the bacterial terminal complex is discussed.
journal_name
Proc Natl Acad Sci U S Aauthors
Hu SQ,Gao YG,Tajima K,Sunagawa N,Zhou Y,Kawano S,Fujiwara T,Yoda T,Shimura D,Satoh Y,Munekata M,Tanaka I,Yao Mdoi
10.1073/pnas.1000601107subject
Has Abstractpub_date
2010-10-19 00:00:00pages
17957-61issue
42eissn
0027-8424issn
1091-6490pii
1000601107journal_volume
107pub_type
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