2MQ8

Solution NMR Structure of De novo designed protein LFR1 1 with ferredoxin fold, Northeast Structural Genomics Consortium (NESG) Target OR414

Summary for 2MQ8

• Entry DOI: 10.2210/pdb2mq8/pdb
• NMR Information: BMRB: 25018
• Descriptor: De novo designed protein LFR1 (1 entity in total)
• Functional Keywords: structural genomics, northeast structural genomics consortium, nesg, psi-biology, protein structure initiative, de novo protein
• Biological source: artificial gene
• Total number of polymer chains: 1
• Total formula weight: 13116.76

Authors

Liu, G.,Lin, Y.,Koga, N.,Koga, R.,Xiao, R.,Janjua, H.,Pederson, K.,Acton, T.B.,Kornhaber, G.,Everett, J.K.,Baker, D.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2014-06-12, release date: 2014-08-20, Last modification date: 2024-05-15)

Primary citation

Lin, Y.R.,Koga, N.,Tatsumi-Koga, R.,Liu, G.,Clouser, A.F.,Montelione, G.T.,Baker, D.
Control over overall shape and size in de novo designed proteins.
Proc.Natl.Acad.Sci.USA, 112:E5478-E5485, 2015

PubMed Abstract: We recently described general principles for designing ideal protein structures stabilized by completely consistent local and nonlocal interactions. The principles relate secondary structure patterns to tertiary packing motifs and enable design of different protein topologies. To achieve fine control over protein shape and size within a particular topology, we have extended the design rules by systematically analyzing the codependencies between the lengths and packing geometry of successive secondary structure elements and the backbone torsion angles of the loop linking them. We demonstrate the control afforded by the resulting extended rule set by designing a series of proteins with the same fold but considerable variation in secondary structure length, loop geometry, β-strand registry, and overall shape. Solution NMR structures of four designed proteins for two different folds show that protein shape and size can be precisely controlled within a given protein fold. These extended design principles provide the foundation for custom design of protein structures performing desired functions.

PubMed: 26396255
DOI: 10.1073/pnas.1509508112

Experimental method

SOLUTION NMR