PDBsum entry 3k1k

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Luminescent protein/immune system PDB id
Protein chains
225 a.a. *
114 a.a. *
Waters ×407
* Residue conservation analysis
PDB id:
Name: Luminescent protein/immune system
Title: Green fluorescent protein bound to minimizer nanobody
Structure: Green fluorescent protein. Chain: a, b. Engineered: yes. Mutation: yes. Enhancer. Chain: c, d. Engineered: yes
Source: Aequorea victoria. Organism_taxid: 6100. Gene: gfp. Expressed in: escherichia coli. Expression_system_taxid: 562. Camelus dromedarius. Organism_taxid: 9838.
2.15Å     R-factor:   0.215     R-free:   0.255
Authors: A.Kirchhofer,J.Helma,K.Schmidthals,C.Frauer,S.Cui,A.Karcher, S.Muyldermans,C.C.Delucci,M.C.Cardoso,H.Leonhardt,K.-P.Hopf U.Rothbauer
Key ref: A.Kirchhofer et al. (2010). Modulation of protein properties in living cells using nanobodies. Nat Struct Mol Biol, 17, 133-138. PubMed id: 20010839
28-Sep-09     Release date:   08-Dec-09    
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Protein chains
Pfam   ArchSchema ?
P42212  (GFP_AEQVI) -  Green fluorescent protein
238 a.a.
225 a.a.*
Protein chains
No UniProt id for this chain
Struc: 114 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cellular_component   1 term 
  Biological process     generation of precursor metabolites and energy   3 terms 
  Biochemical function     molecular_function     1 term  


Nat Struct Mol Biol 17:133-138 (2010)
PubMed id: 20010839  
Modulation of protein properties in living cells using nanobodies.
A.Kirchhofer, J.Helma, K.Schmidthals, C.Frauer, S.Cui, A.Karcher, M.Pellis, S.Muyldermans, C.S.Casas-Delucchi, M.C.Cardoso, H.Leonhardt, K.P.Hopfner, U.Rothbauer.
Protein conformation is critically linked to function and often controlled by interactions with regulatory factors. Here we report the selection of camelid-derived single-domain antibodies (nanobodies) that modulate the conformation and spectral properties of the green fluorescent protein (GFP). One nanobody could reversibly reduce GFP fluorescence by a factor of 5, whereas its displacement by a second nanobody caused an increase by a factor of 10. Structural analysis of GFP-nanobody complexes revealed that the two nanobodies induce subtle opposing changes in the chromophore environment, leading to altered absorption properties. Unlike conventional antibodies, the small, stable nanobodies are functional in living cells. Nanobody-induced changes were detected by ratio imaging and used to monitor protein expression and subcellular localization as well as translocation events such as the tamoxifen-induced nuclear localization of estrogen receptor. This work demonstrates that protein conformations can be manipulated and studied with nanobodies in living cells.