1EM7

HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G

Summary for 1EM7

• Entry DOI: 10.2210/pdb1em7/pdb
• Related: 1gb4 1pga
• Descriptor: PROTEIN G (2 entities in total)
• Functional Keywords: helix propensity, helix dipole interaction, protein design, protein g, membrane protein
• Biological source: Streptococcus sp.
• Cellular location: Secreted, cell wall ; Peptidoglycan-anchor : P06654
• Total number of polymer chains: 1
• Total formula weight: 6287.90

Authors

Strop, P.,Marinescu, A.M.,Mayo, S.L. (deposition date: 2000-03-16, release date: 2002-05-08, Last modification date: 2024-02-07)

Primary citation

Strop, P.,Marinescu, A.M.,Mayo, S.L.
Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design.
Protein Sci., 9:1391-1394, 2000

PubMed Abstract: 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.

PubMed: 10933505

Experimental method

X-RAY DIFFRACTION (2 Å)