1em7
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1em7.jpg|left|200px]] | + | [[Image:1em7.jpg|left|200px]] |
| - | + | ||
| - | '''HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G''' | + | {{Structure |
| + | |PDB= 1em7 |SIZE=350|CAPTION= <scene name='initialview01'>1em7</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1EM7 is a [ | + | 1EM7 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=1EM7 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design., Strop P, Marinescu AM, Mayo SL, Protein Sci. 2000 Jul;9(7):1391-4. PMID:[http:// | + | Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design., Strop P, Marinescu AM, Mayo SL, Protein Sci. 2000 Jul;9(7):1391-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10933505 10933505] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus sp.]] | [[Category: Streptococcus sp.]] | ||
| Line 21: | Line 30: | ||
[[Category: protein g]] | [[Category: 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 10:57:28 2008'' |
Revision as of 08:57, 20 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G
Overview
Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gbeta1m2 suggests that the increased stability of Gbeta1m2 is due to increased helix propensity and more favorable helix dipole interactions.
About this Structure
1EM7 is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
Reference
Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design., Strop P, Marinescu AM, Mayo SL, Protein Sci. 2000 Jul;9(7):1391-4. PMID:10933505
Page seeded by OCA on Thu Mar 20 10:57:28 2008
