2GB1

A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G

Summary for 2GB1

• Entry DOI: 10.2210/pdb2gb1/pdb
• Descriptor: PROTEIN G (1 entity in total)
• Functional Keywords: immunoglobulin binding protein
• Biological source: Streptococcus sp. 'group G'
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654
• Total number of polymer chains: 1
• Total formula weight: 6201.78

Authors

Gronenborn, A.M.,Clore, G.M. (deposition date: 1991-05-15, release date: 1993-04-15, Last modification date: 2024-05-29)

Primary citation

Gronenborn, A.M.,Filpula, D.R.,Essig, N.Z.,Achari, A.,Whitlow, M.,Wingfield, P.T.,Clore, G.M.
A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.
Science, 253:657-661, 1991

PubMed Abstract: The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C).

PubMed: 1871600

Experimental method

SOLUTION NMR