1gb4
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1gb4.gif|left|200px]] | + | [[Image:1gb4.gif|left|200px]] |
| - | + | ||
| - | '''HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1gb4 |SIZE=350|CAPTION= <scene name='initialview01'>1gb4</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= GB1C3B4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1306 Streptococcus sp.]) | ||
| + | }} | ||
| + | |||
| + | '''HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1GB4 is a [ | + | 1GB4 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=1GB4 OCA]. |
==Reference== | ==Reference== | ||
| - | Design, structure and stability of a hyperthermophilic protein variant., Malakauskas SM, Mayo SL, Nat Struct Biol. 1998 Jun;5(6):470-5. PMID:[http:// | + | Design, structure and stability of a hyperthermophilic protein variant., Malakauskas SM, Mayo SL, Nat Struct Biol. 1998 Jun;5(6):470-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9628485 9628485] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus sp.]] | [[Category: Streptococcus sp.]] | ||
| Line 18: | Line 27: | ||
[[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 11:20:43 2008'' |
Revision as of 09:20, 20 March 2008
| |||||||
| Gene: | GB1C3B4 (Streptococcus sp.) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES
Overview
Here we report the use of an objective computer algorithm in the design of a hyperstable variant of the Streptococcal protein Gbeta1 domain (Gbeta1). The designed seven-fold mutant, Gbeta1-c3b4, has a melting temperature in excess of 100 degrees C and an enhancement in thermodynamic stability of 4.3 kcal mol(-1) at 50 degrees C over the wild-type protein. Gbeta1-c3b4 maintains the Gbeta1 fold, as determined by nuclear magnetic resonance spectroscopy, and also retains a significant level of binding to human IgG in qualitative comparisons with wild type. The basis of the stability enhancement appears to have multiple components including optimized core packing, increased burial of hydrophobic surface area, more favorable helix dipole interactions, and improvement of secondary structure propensity. The design algorithm is able to model such complex contributions simultaneously using empirical physical/chemical potential functions and a combinatorial optimization algorithm based on the dead-end elimination theorem. Because the design methodology is based on general principles, there is the potential of applying the methodology to the stabilization of other unrelated protein folds.
About this Structure
1GB4 is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
Reference
Design, structure and stability of a hyperthermophilic protein variant., Malakauskas SM, Mayo SL, Nat Struct Biol. 1998 Jun;5(6):470-5. PMID:9628485
Page seeded by OCA on Thu Mar 20 11:20:43 2008
