4KY3

Three-dimensional Structure of the orthorhombic crystal of computationally designed insertion domain , Northeast Structural Genomics Consortium (NESG) Target OR327

Summary for 4KY3

• Entry DOI: 10.2210/pdb4ky3/pdb
• Descriptor: designed protein OR327 (1 entity in total)
• Functional Keywords: structural genomics, psi-biology, protein structure initiative, northeast structural genomics consortium, nesg, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 3
• Total formula weight: 59528.92

Authors

Kuzin, A.,Su, M.,Seetharaman, J.,Maglaqui, M.,Xiao, R.,Lee, D.,Gleixner, J.,Baker, D.,Everett, J.K.,Acton, T.B.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2013-05-28, release date: 2013-06-19, Last modification date: 2024-10-30)

Primary citation

King, I.C.,Gleixner, J.,Doyle, L.,Kuzin, A.,Hunt, J.F.,Xiao, R.,Montelione, G.T.,Stoddard, B.L.,DiMaio, F.,Baker, D.
Precise assembly of complex beta sheet topologies from de novo designed building blocks.
Elife, 4:-, 2015

PubMed Abstract: Design of complex alpha-beta protein topologies poses a challenge because of the large number of alternative packing arrangements. A similar challenge presumably limited the emergence of large and complex protein topologies in evolution. Here, we demonstrate that protein topologies with six and seven-stranded beta sheets can be designed by insertion of one de novo designed beta sheet containing protein into another such that the two beta sheets are merged to form a single extended sheet, followed by amino acid sequence optimization at the newly formed strand-strand, strand-helix, and helix-helix interfaces. Crystal structures of two such designs closely match the computational design models. Searches for similar structures in the SCOP protein domain database yield only weak matches with different beta sheet connectivities. A similar beta sheet fusion mechanism may have contributed to the emergence of complex beta sheets during natural protein evolution.

PubMed: 26650357
DOI: 10.7554/eLife.11012

Experimental method

X-RAY DIFFRACTION (2.964 Å)