Hidden order in the GroEL-GroES-(ADP)7 chaperonin: forms, folding, and ADP-binding sites.
A molecular crystallography approach reveals the existence of a hidden order in GroEL-GroES-(ADP)(7). The new crystallographic symmetry concepts required are first illustrated for a hypothetical planar molecule. Their application to the chaperonin complex leads to molecular forms with vertices having integral coordinates (the indices) with respect to a symmetry-adapted basis and to folding points approximated by ideal C(alpha) positions with rational indices connected by integral scale-rotations, just as for the vertices of the molecular forms. The Mg(+2)-ions at nucleotide binding sites are symmetry-related in a similar way to C(alpha)'s folding points.
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Institute for Theoretical Physics, University of Nijmegen, Toernooiveld, Nijmegen, The Netherlands. alo@sci.kun.nl
D000244:Adenosine Diphosphate / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018835:Chaperonin 10 / Q000737:chemistry* / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances; D008958:Models, Molecular; D008968:Molecular Conformation; D017510:Protein Folding
D018835:Chaperonin 10; D018834:Chaperonin 60; D046911:Macromolecular Substances; D000244:Adenosine Diphosphate