1em7 | pdb_00001em7

HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G

spinqualitylabelsall models 1em7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1em7 is a 1 chain structure with sequence from Streptococcus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1gb4, 1pga Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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