2onq
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= spg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1306 Streptococcus sp.]) | |GENE= spg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1306 Streptococcus sp.]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2on8|2ON8]], [[1pga|1PGA]], [[1gb4|1GB4]], [[1fcc|1FCC]], [[3gb1|3GB1]], [[1p7e|1P7E]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2onq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2onq OCA], [http://www.ebi.ac.uk/pdbsum/2onq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2onq RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: protein binding]] | [[Category: protein binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:20:32 2008'' |
Revision as of 01:20, 31 March 2008
| |||||||
| , resolution 1.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | spg (Streptococcus sp.) | ||||||
| Related: | 2ON8, 1PGA, 1GB4, 1FCC, 3GB1, 1P7E
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Gbeta1 stabilization by in vitro evolution and computational design
Overview
Computational design and in vitro evolution are major strategies for stabilizing proteins. For the four critical positions 16, 18, 25, and 29 of the B domain of the streptococcal protein G (Gbeta1), they identified the same optimal residues at positions 16 and 25, but not at 18 and 29. Here we analyzed the energetic contributions of the residues from these two approaches by single and double mutant analyses and determined crystal structures for a variant from the calculation (I16/L18/E25/K29) and from the selection (I16/I18/E25/F29). The structural analysis explains the observed differences in stabilization. Residues 16, 18, and 29 line an invagination, which results from a packing defect between the helix and the beta-sheet of Gbeta1. In all stabilized variants, residues with larger side-chains occur at these positions and packing is improved. In the selected variant, packing is better optimized than in the computed variant. Such differences in side-chain packing strongly affect stability but are difficult to evaluate by computation.
About this Structure
2ONQ is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
Reference
Optimization of the gbeta1 domain by computational design and by in vitro evolution: structural and energetic basis of stabilization., Wunderlich M, Max KE, Roske Y, Mueller U, Heinemann U, Schmid FX, J Mol Biol. 2007 Oct 26;373(3):775-84. Epub 2007 Aug 19. PMID:17868696
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