Summary for 3AJ2
| Entry DOI | 10.2210/pdb3aj2/pdb |
| Related | 2Z9E 3AJ1 |
| Descriptor | Cellulose synthase operon protein D (2 entities in total) |
| Functional Keywords | alpha and beta fold, octamer, tetramer of dimers, molecule ring, cellulose biosynthesis, structural genomics, nppsfa, national project on protein structural and functional analyses, biosynthetic protein |
| Biological source | Acetobacter xylinus (Gluconacetobacter xylinus) |
| Total number of polymer chains | 4 |
| Total formula weight | 72870.86 |
| Authors | Hu, S.Q.,Tajima, K.,Zhou, Y.,Tanaka, I.,Yao, M. (deposition date: 2010-05-20, release date: 2010-10-06, Last modification date: 2023-11-01) |
| Primary citation | Hu, S.Q.,Gao, Y.G.,Tajima, K.,Sunagawa, N.,Zhou, Y.,Kawano, S.,Fujiwara, T.,Yoda, T.,Shimura, D.,Satoh, Y.,Munekata, M.,Tanaka, I.,Yao, M. Structure of bacterial cellulose synthase subunit D octamer with four inner passageways Proc.Natl.Acad.Sci.USA, 107:17957-17961, 2010 Cited by PubMed 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. PubMed: 20921370DOI: 10.1073/pnas.1000601107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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