2Q6P

The Chemical Control of Protein Folding: Engineering a Superfolder Green Fluorescent Protein

Summary for 2Q6P

Entry DOI	10.2210/pdb2q6p/pdb
Descriptor	Green fluorescent protein mutant 3 (2 entities in total)
Functional Keywords	gfp, noncanonical amino acid, superfolder, luminescent protein
Biological source	Aequorea victoria
Total number of polymer chains	1
Total formula weight	27091.28
Authors	Steiner, T.,Hess, P.,Bae, J.H.,Wiltschi, B.,Moroder, L.,Budisa, N. (deposition date: 2007-06-05, release date: 2007-06-19, Last modification date: 2024-11-13)
Primary citation	Steiner, T.,Hess, P.,Bae, J.H.,Wiltschi, B.,Moroder, L.,Budisa, N. Synthetic biology of proteins: tuning GFPs folding and stability with fluoroproline. Plos One, 3:e1680-e1680, 2008 Cited by PubMed Abstract: Proline residues affect protein folding and stability via cis/trans isomerization of peptide bonds and by the C(gamma)-exo or -endo puckering of their pyrrolidine rings. Peptide bond conformation as well as puckering propensity can be manipulated by proper choice of ring substituents, e.g. C(gamma)-fluorination. Synthetic chemistry has routinely exploited ring-substituted proline analogs in order to change, modulate or control folding and stability of peptides. PubMed: 18301757 DOI: 10.1371/journal.pone.0001680 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation