PDBsum entry 3rg6

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Top Page protein Protein-protein interface(s) links
Photosynthesis PDB id
Protein chains
442 a.a.
115 a.a.
107 a.a.

References listed in PDB file
Key reference
Title Crystal structure of a chaperone-Bound assembly intermediate of form i rubisco.
Authors A.Bracher, A.Starling-Windhof, F.U.Hartl, M.Hayer-Hartl.
Ref. Nat Struct Mol Biol, 2011, 18, 875-880.
PubMed id 21765418
No abstract given.
Secondary reference #1
Title Coupled chaperone action in folding and assembly of hexadecameric rubisco.
Authors C.Liu, A.L.Young, A.Starling-Windhof, A.Bracher, S.Saschenbrecker, B.V.Rao, K.V.Rao, O.Berninghausen, T.Mielke, F.U.Hartl, R.Beckmann, M.Hayer-Hartl.
Ref. Nature, 2010, 463, 197-202. [DOI no: 10.1038/nature08651]
PubMed id 20075914
Full text Abstract
Figure 4.
Figure 4: RbcX[2]–RbcL interactions. a, Close-up of a top view of RbcL[8]–(RbcX[2])[8] (yellow mesh) showing the RbcL C terminus (red, residues 413–475) interacting with RbcX[2] (gold) (dashed box Fig. 3g). The RbcL C terminus is shown with the conserved residues F467 and F469 inserting into the hydrophobic binding pockets of RbcX[2]. b, Close-up of a side view of RbcL[8]–(RbcX[2])[8] with RbcX[2] interacting with the N-terminal domain of an adjacent RbcL (dashed box Fig. 3h). Conserved RbcX[2] residues Q29, E32, T33 and N34 are shown as blue spheres; candidate regions on RbcL for interaction with RbcX[2] are in pink. The C-terminal sequence of the adjacent RbcL reaching into the groove of RbcX[2] is seen in the background (red). c, Crosslinking of Syn6301-RbcL[8]–AnaCA-(RbcX[2])[8] complex. Isolated complex with RbcX[2] containing pBpa at the positions indicated was exposed to ultraviolet light (UV) and analysed together with non-exposed controls by anti-RbcL immunoblotting. Photoadducts are indicated by open arrowheads. Control, RbcL[8]–(RbcX[2])[8] complex without crosslinker. In the ribbon diagram of form II AnaCA-RbcX[2], amino-acid positions (labelled in one chain) that resulted in crosslinking are shown in blue and non-reactive positions in red.
Figure 6.
Figure 6: Model of GroEL/ES and RbcX[2]-assisted folding and assembly of Rubisco. a, Folded RbcL with a disordered C-terminal region is transiently released from the GroEL/GroES. b, RbcX[2] binds to the exposed RbcL C terminus, c, RbcL dimers are formed, ‘stapled’ together by the interaction of RbcX[2] with the C terminus of one RbcL and the N-terminal domain of the adjacent subunit. d, Stable dimers assemble to RbcL[8]–(RbcX[2])[8] complexes. e, RbcS binding weakens the RbcL–RbcX[2] interaction. Dissociation of RbcX[2] and binding of RbcS may occur in a stepwise manner, populating intermediates. f, RbcX[2] dissociates, enabling the C-terminal region of RbcL to adopt its final position and allowing maturation of Rubisco.
The above figures are reproduced from the cited reference with permission from Macmillan Publishers Ltd
Secondary reference #2
Title Structure and function of rbcx, An assembly chaperone for hexadecameric rubisco.
Authors S.Saschenbrecker, A.Bracher, K.V.Rao, B.V.Rao, F.U.Hartl, M.Hayer-Hartl.
Ref. Cell, 2007, 129, 1189-1200. [DOI no: 10.1016/j.cell.2007.04.025]
PubMed id 17574029
Full text Abstract
Figure 4.
Figure 4. Binding of C-Terminal RbcL Peptide to RbcX
(A) A cellulose membrane containing an array of overlapping dodecamer peptides covering the sequence of Syn7002-RbcL was probed with the RbcX proteins indicated. Peptide-bound RbcX was visualized by chemiluminescent immunodetection with anti-RbcX antibody.
(B) Alignment using MultAlin (Corpet, 1988) of C-terminal amino acid sequences of RbcL from the cyanobacterial and higher plant species indicated (Swiss-Prot accession numbers in brackets). High consensus level (≥ 90%) is depicted in red and low consensus level (≥ 50%) in blue.
(C) Structure of the complex of peptide EIKFEFD bound to RbcX dimer. The peptide is shown in stick representation; RbcX is represented as a molecular surface with protomers colored white and blue, respectively. N and C termini of the peptide are indicated.
(D) Magnification of boxed area in (C) presenting a view of the refined peptide bound to RbcX. Molecular interactions between peptide and RbcX are highlighted. Dashed lines represent hydrogen bonds. Residues of the RbcX monomers participating in peptide binding are displayed in stick representation below the transparent surface of the molecule and are numbered in white and yellow, respectively. The important hydrophobic residues in the bound peptide are also labeled.
Figure 7.
Figure 7. Working Model of RbcX Function in Cyanobacterial Rubisco Assembly
RbcX functions to increase the efficiency of Rubisco assembly by acting on folded RbcL subunits subsequent to their GroEL/GroES-mediated folding. Recognition of RbcX requires the exposed C-terminal RbcL peptide (see Discussion for details and Figure S11). Note that assembly of RbcL[8]S[8] may also occur independently of RbcX for some Rubisco homologs, presumably involving similar assembly intermediates.
The above figures are reproduced from the cited reference with permission from Cell Press
Secondary reference #3
Title Structure determination and refinement of ribulose 1,5-Bisphosphate carboxylase/oxygenase from synechococcus pcc6301.
Authors J.Newman, C.I.Branden, T.A.Jones.
Ref. Acta Crystallogr D Biol Crystallogr, 1993, 49, 548-560. [DOI no: 10.1107/S090744499300530X]
PubMed id 15299492
Full text Abstract
Figure 9.
Fig. 9. A ribbon diagram of an/,2 dimer. The barrel of one L subunit is coloured blue, and the N-terminal domain of the same subunit, cyan. The barrel domain of the second L subunit is red, and its N-terminal domain is magenta. The yellow spheres are Mg 2 ions, and show the positions of the active sites. Both this figure and the previous figure were generated in O.
Figure 15.
Fig. 15. Pepflip values versus residue number. The dashed line shows the 2.5 threshold suggested by Jones et al. Table 3 summarizes the residues which have~ a pepflip >__ 2.5.
The above figures are reproduced from the cited reference with permission from the IUCr
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