1FCL

DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G

Summary for 1FCL

• Entry DOI: 10.2210/pdb1fcl/pdb
• Related: 1FD6 1GB1 1GB4
• NMR Information: BMRB: 5152
• Descriptor: IMMUNOGLOBULIN G BINDING PROTEIN G (1 entity in total)
• Functional Keywords: designed core mutant, streptococcal protein g, protein binding
• Biological source: Streptococcus sp.
• Total number of polymer chains: 1
• Total formula weight: 6216.82

Authors

Ross, S.A.,Sarisky, C.A.,Su, A.,Mayo, S.L. (deposition date: 2000-07-18, release date: 2001-09-19, Last modification date: 2024-05-22)

Primary citation

Ross, S.A.,Sarisky, C.A.,Su, A.,Mayo, S.L.
Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification.
Protein Sci., 10:450-454, 2001

PubMed Abstract: The solution structures of two computationally designed core variants of the beta 1 domain of streptococcal protein G (G beta 1) were solved by (1)H NMR methods to assess the robustness of amino acid sequence selection by the ORBIT protein design package under changes in protein backbone specification. One variant has mutations at three of 10 core positions and corresponds to minimal perturbations of the native G beta 1 backbone. The other, with mutations at six of 10 positions, was calculated for a backbone in which the separation between G beta 1's alpha-helix and beta-sheet was increased by 15% relative to native G beta 1. Exchange broadening of some resonances and the complete absence of others in spectra of the sixfold mutant bespeak conformational heterogeneity in this protein. The NMR data were sufficiently abundant, however, to generate structures of similar, moderately high quality for both variants. Both proteins adopt backbone structures similar to their target folds. Moreover, the sequence selection algorithm successfully predicted all core chi(1) angles in both variants, five of six chi(2) angles in the threefold mutant and four of seven chi(2) angles in the sixfold mutant. We conclude that ORBIT calculates sequences that fold specifically to a geometry close to the template, even when the template is moderately perturbed relative to a naturally occurring structure. There are apparently limits to the size of acceptable perturbations: In this study, the larger perturbation led to undesired dynamic behavior.

PubMed: 11266631
DOI: 10.1110/ps.32501

Experimental method

SOLUTION NMR