4GPM
Crystal Structure of Engineered Protein. Northeast Structural Genomics Consortium Target OR264.
Summary for 4GPM
| Entry DOI | 10.2210/pdb4gpm/pdb |
| Related | 4GMR |
| Descriptor | Engineered Protein OR264 (2 entities in total) |
| Functional Keywords | de novo protein, structural genomics, psi-biology, northeast structural genomics consortium, nesg |
| Biological source | synthetic construct |
| Total number of polymer chains | 2 |
| Total formula weight | 36704.59 |
| Authors | Vorobiev, S.,Su, M.,Parmeggiani, F.,Seetharaman, J.,Huang, P.-S.,Maglaqui, M.,Xiao, R.,Lee, D.,Everett, J.K.,Acton, T.B.,Baker, D.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2012-08-21, release date: 2012-09-05, Last modification date: 2023-09-13) |
| Primary citation | Fallas, J.A.,Ueda, G.,Sheffler, W.,Nguyen, V.,McNamara, D.E.,Sankaran, B.,Pereira, J.H.,Parmeggiani, F.,Brunette, T.J.,Cascio, D.,Yeates, T.R.,Zwart, P.,Baker, D. Computational design of self-assembling cyclic protein homo-oligomers. NAT.CHEM., 9:353-360, 2017 Cited by PubMed Abstract: Self-assembling cyclic protein homo-oligomers play important roles in biology, and the ability to generate custom homo-oligomeric structures could enable new approaches to probe biological function. Here we report a general approach to design cyclic homo-oligomers that employs a new residue-pair-transform method to assess the designability of a protein-protein interface. This method is sufficiently rapid to enable the systematic enumeration of cyclically docked arrangements of a monomer followed by sequence design of the newly formed interfaces. We use this method to design interfaces onto idealized repeat proteins that direct their assembly into complexes that possess cyclic symmetry. Of 96 designs that were characterized experimentally, 21 were found to form stable monodisperse homo-oligomers in solution, and 15 (four homodimers, six homotrimers, six homotetramers and one homopentamer) had solution small-angle X-ray scattering data consistent with the design models. X-ray crystal structures were obtained for five of the designs and each is very close to their corresponding computational model. PubMed: 28338692DOI: 10.1038/nchem.2673 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.002 Å) |
Structure validation
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