1fcl
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1fcl.gif|left|200px]] | + | [[Image:1fcl.gif|left|200px]] |
| - | + | ||
| - | '''DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G''' | + | {{Structure |
| + | |PDB= 1fcl |SIZE=350|CAPTION= <scene name='initialview01'>1fcl</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1FCL is a [ | + | 1FCL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCL OCA]. |
==Reference== | ==Reference== | ||
| - | Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification., Ross SA, Sarisky CA, Su A, Mayo SL, Protein Sci. 2001 Feb;10(2):450-4. PMID:[http:// | + | Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification., Ross SA, Sarisky CA, Su A, Mayo SL, Protein Sci. 2001 Feb;10(2):450-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11266631 11266631] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus sp.]] | [[Category: Streptococcus sp.]] | ||
| Line 20: | Line 29: | ||
[[Category: streptococcal protein g]] | [[Category: streptococcal protein g]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:07:23 2008'' |
Revision as of 09:07, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G
Overview
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.
About this Structure
1FCL is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
Reference
Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification., Ross SA, Sarisky CA, Su A, Mayo SL, Protein Sci. 2001 Feb;10(2):450-4. PMID:11266631
Page seeded by OCA on Thu Mar 20 11:07:23 2008
