1ZXG

Solution structure of A219

Summary for 1ZXG

• Entry DOI: 10.2210/pdb1zxg/pdb
• Descriptor: Immunoglobulin G binding protein A (1 entity in total)
• Functional Keywords: igg-binding, protein a, phage display, immune system-protein binding complex, immune system/protein binding
• Biological source: Staphylococcus aureus
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q53759
• Total number of polymer chains: 1
• Total formula weight: 6733.48

Authors

He, Y.,Yeh, D.C.,Alexander, P.,Bryan, P.N.,Orban, J. (deposition date: 2005-06-08, release date: 2005-11-08, Last modification date: 2024-05-22)

Primary citation

He, Y.,Yeh, D.C.,Alexander, P.,Bryan, P.N.,Orban, J.
Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds.
Biochemistry, 44:14055-14061, 2005

PubMed Abstract: We describe here the solution NMR structures of two IgG binding domains with highly homologous sequences but different three-dimensional structures. The proteins, G311 and A219, are derived from the IgG binding domains of their wild-type counterparts, protein G and protein A, respectively. Through a series of site-directed mutations and phage display selections, the sequences of G311 and A219 were designed to converge to a point of high-level sequence identity while keeping their respective wild-type tertiary folds. Structures of both artificially evolved sequences were determined by NMR spectroscopy. The main chain fold of G311 can be superimposed on the wild-type alpha/beta protein G structure with a backbone rmsd of 1.4 A, and the A219 structure can be overlaid on the wild-type three-alpha-helix protein A fold also with a backbone rmsd of 1.4 A. The structure of G311, in particular, accommodates a large number of mutational changes without undergoing a change in the overall fold of the main chain. The structural differences are maintained despite a high level (59%) of sequence identity. These proteins serve as starting points for further experiments that will probe basic concepts of protein folding and conformational switching.

PubMed: 16245921
DOI: 10.1021/bi051232j

Experimental method

SOLUTION NMR