The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.
GroEL is a bacterial chaperonin of 14 identical subunits required to help fold newly synthesized proteins. The crystal structure of GroEL with ATP gamma S bound to each subunit shows that ATP binds to a novel pocket, whose primary sequence is highly conserved among chaperonins. Interaction of Mg2+ and ATP involves phosphate oxygens of the alpha-, beta- and gamma-phosphates, which is unique for known structures of nucleotide-binding proteins. Although bound ATP induces modest conformational shifts in the equatorial domain, the stereochemistry that functionally coordinates GroEL's affinity for nucleotides, polypeptide, and GroES remains uncertain.
Boisvert
D C
DC
Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
Wang
J
J
Otwinowski
Z
Z
Horwich
A L
AL
Sigler
P B
PB
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
D018834:Chaperonin 60; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate; D008274:Magnesium