PDBsum entry 2c7c

Chaperone

PDB id: 2c7c

Contents

Protein chains

(+ 8 more) 525 a.a. *

(+ 1 more) 93 a.a. *

* Residue conservation analysis

PDB id:

2c7c

Name:

Chaperone

Title:

Fitted coordinates for groel-atp7-groes cryo-em complex (emd-1180)

Structure:

60 kda chaperonin. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Synonym: groel, protein cpn60, groel protein. Engineered: yes. 10 kda chaperonin molecule: groes, protein cpn10, groes protein. Chain: o, p, q, r, s, t, u. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Biol. unit:

21mer (from PQS)

Authors:

N.A.Ranson,D.K.Clare,G.W.Farr,D.Houldershaw,A.L.Horwich,H.R.Saibil

Key ref:

N.A.Ranson et al. (2006). Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nat Struct Mol Biol, 13, 147-152. PubMed id: 16429154 DOI: 10.1038/nsmb1046

Date:

22-Nov-05 Release date: 25-Jan-06

Protein chains

P0A6F5  (CH60_ECOLI) -  Chaperonin GroEL from Escherichia coli (strain K12)

Seq: 548 a.a.

Struc: 525 a.a.

Protein chains

P0A6F9  (CH10_ECOLI) -  Co-chaperonin GroES from Escherichia coli (strain K12)

Seq: 97 a.a.

Struc: 93 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N: E.C.5.6.1.7 - chaperonin ATPase.
• Reaction: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
• Enzyme class 3: Chains O, P, Q, R, S, T, U: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1038/nsmb1046

Nat Struct Mol Biol 13:147-152 (2006)

PubMed id: 16429154

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.

N.A.Ranson, D.K.Clare, G.W.Farr, D.Houldershaw, A.L.Horwich, H.R.Saibil.

ABSTRACT

The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.

Selected figure(s)

Figure 2.
Figure 2. Solution structures of GroEL–ATP[7]–GroES and GroEL–ADP[7]–GroES. (a) Surface representation of the side view of the GroEL–ATP[7]–GroES complex. (b) Surface representation of the side view of the GroEL–ADP[7]–GroES complex. (c,d) Central sections through the cryo-EM maps are shown as a semitransparent surface in either gold (c; ATP) or blue (d; ADP), with the atomic coordinates for the GroEL equatorial (green; residues 3–136 and 410–524), intermediate (yellow; residues 137–191 and 374–409), apical (red; residues 192–373, except for 353–361 at the tip of the mobile helical hairpin in the trans ring) and GroES (magenta) fitted in. The seven-fold axis of the GroEL–GroES oligomer is vertical and in the image plane for all figures. The resolutions of the ATP- and ADP-bound maps are 7.7 Å and 8.7 Å, respectively, determined by Fourier shell correlation at a cutoff of 0.5. Fourier shell correlation curves for both reconstructions are shown in Supplementary Figure 1.

Figure 4.
Figure 4. Disruption of intra-ring contacts between the equatorial domains of the trans ring. (a) The interface between neighboring equatorial domains in the trans ring of the ATP-bound complex. The EM-derived electron density is shown as a gold mesh, with the adjacent equatorial domains in blue and magenta. In the ATP complex (and all crystal structures of GroEL complexes), two -strands from each subunit form a four-stranded -sheet that is a major contact holding the ring of equatorial domains together (highlighted by a black rectangle). (b) The corresponding view of the ADP-bound complex (with EM density shown as a blue mesh and equatorial domains in green and orange) shows that a small ( 3°) rotation of the equatorial domain results in the two strands from the orange subunit moving upward (in this view) and the two strands from the green subunit moving downward, pulling apart the -sheet contact. (c,d) Structure of the rear half of the ring of equatorial domains from the ATP-bound (c) and ADP-bound (d) complexes. The seven-fold axis is vertical and in the image plane, and these views are reached by tipping a and b forward by 30°. (e) A comparison of the intra-strand (main chain) distances in the ATP (blue and magenta) and ADP (green and gold) complexes, showing that the strand separation increases by 4–5 Å upon ATP hydrolysis.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2006, 13, 147-152) copyright 2006.

Figures were selected by an automated process.