Database accession: MF7000855
Name: AtRbcX2 (Arabidopsis thaliana)
PDB ID: 4gr6
Experimental method: X-ray (2.00 Å)
Assembly: Homodimer
Source organism: Arabidopsis thaliana
Primary publication of the structure:
Kolesinski P, Golik P, Grudnik P, Piechota J, Markiewicz M, Tarnawski M, Dubin G, Szczepaniak A
Insights into eukaryotic Rubisco assembly - crystal structures of RbcX chaperones from Arabidopsis thaliana.
(2013) Biochim. Biophys. Acta 1830: 2899-906
PMID: 23295968
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
protein folding chaperone protein folding chaperone
Biological process:
carbon fixation carbon fixation
chaperone-mediated protein folding chaperone-mediated protein folding
photosynthesis photosynthesis
ribulose bisphosphate carboxylase complex assembly ribulose bisphosphate carboxylase complex assembly
Cellular component:
chloroplast stroma chloroplast stroma
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Chaperonin-like RbcX protein 2, chloroplastic
Source organism: Arabidopsis thaliana
Length: 203 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMVSAWFVVGSPVMDSSSSPCLCLDAHTTGTIRRKKILGKARNLELGSSFTGSRIVFRLSPKRVSRIANRKSKKLLIVNEDVAGNYDDTFGDVQKQIVNYFTYKAVRTVLHQLYEMNPPQYTWFYNHIITNRPTDGKRFLRALGKESQELAERVMITRLHLYGKWIKKCDHGKIYQEISDENLALMRERLMETVIWPSDDTNSR
UniProtKB AC: Q8L9X2 (positions: 88-191)
Coverage: 51%
Name: Chaperonin-like RbcX protein 2, chloroplastic
Source organism: Arabidopsis thaliana
Length: 203 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMVSAWFVVGSPVMDSSSSPCLCLDAHTTGTIRRKKILGKARNLELGSSFTGSRIVFRLSPKRVSRIANRKSKKLLIVNEDVAGNYDDTFGDVQKQIVNYFTYKAVRTVLHQLYEMNPPQYTWFYNHIITNRPTDGKRFLRALGKESQELAERVMITRLHLYGKWIKKCDHGKIYQEISDENLALMRERLMETVIWPSDDTNSR
UniProtKB AC: Q8L9X2 (positions: 88-192)
Coverage: 51%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Chaperonin-like RbcX
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
There is no information on the stability/disoder of the monomeric forms. However, RbcX is a dimer in solution (PMID:17574029) and its biologically relevant form is the homodimer (a monomeric form with this fold is not known PMID:23295968, PMID:21821880). The structure is highly intertwined with the interface being extended and hydrophobic between the two four-helix-bundle cores and by the exchange of the C-terminal parts of the long a4 helices between the two subunits (PMID:21821880).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
