3j03 | pdb_00003j03

Lidless Mm-cpn in the closed state with ATP/AlFx

spinqualitylabelsall models 3j03, resolution 4.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3j03 is a 16 chain structure with sequence from Atcc 43000. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3j02 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Chaperonins are large ATP-driven molecular machines that mediate cellular protein folding. Group II chaperonins use their "built-in lid" to close their central folding chamber. Here we report the structure of an archaeal group II chaperonin in its prehydrolysis ATP-bound state at subnanometer resolution using single particle cryo-electron microscopy (cryo-EM). Structural comparison of Mm-cpn in ATP-free, ATP-bound, and ATP-hydrolysis states reveals that ATP binding alone causes the chaperonin to close slightly with a approximately 45 degrees counterclockwise rotation of the apical domain. The subsequent ATP hydrolysis drives each subunit to rock toward the folding chamber and to close the lid completely. These motions are attributable to the local interactions of specific active site residues with the nucleotide, the tight couplings between the apical and intermediate domains within the subunit, and the aligned interactions between two subunits across the rings. This mechanism of structural changes in response to ATP is entirely different from those found in group I chaperonins. Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.,Zhang J, Ma B, DiMaio F, Douglas NR, Joachimiak LA, Baker D, Frydman J, Levitt M, Chiu W Structure. 2011 May 11;19(5):633-9. PMID:21565698 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin

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