Database accession: MF7000321
Name: AtRbcX1 (Arabidopsis thaliana)
PDB ID: 4gr2
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
response to cold response to cold
response to salt stress response to salt stress
response to water deprivation response to water deprivation
ribulose bisphosphate carboxylase complex assembly ribulose bisphosphate carboxylase complex assembly
Cellular component:
chloroplast thylakoid chloroplast thylakoid
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 1, chloroplastic
Source organism: Arabidopsis thaliana
Length: 174 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMESSSSLLHHSYLSYLNPKFGKRPLVSYPLMQSSRKCKQTRICSNKMYVPGFGEASPEAKAAKHLHDFFTYVAVRIVSAQLESYNPEAYMELREFLDTNSVSDGDKFCATLMRRSSRHMNLALRILEVRSAYCKNDFEWDNMKRLAFKNVDDSNTRLMREYVLETSHVETDSDK
UniProtKB AC: Q94AU9 (positions: 54-163)
Coverage: 63%
Name: Chaperonin-like RBCX protein 1, chloroplastic
Source organism: Arabidopsis thaliana
Length: 174 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMESSSSLLHHSYLSYLNPKFGKRPLVSYPLMQSSRKCKQTRICSNKMYVPGFGEASPEAKAAKHLHDFFTYVAVRIVSAQLESYNPEAYMELREFLDTNSVSDGDKFCATLMRRSSRHMNLALRILEVRSAYCKNDFEWDNMKRLAFKNVDDSNTRLMREYVLETSHVETDSDK
UniProtKB AC: Q94AU9 (positions: 49-166)
Coverage: 67%
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)
