Crystal structure of the C-terminal fragment (residues 756-982 with the C864S mutation) of Arabidopsis thaliana CHUP1Crystal structure of the C-terminal fragment (residues 756-982 with the C864S mutation) of Arabidopsis thaliana CHUP1

Structural highlights

8waf is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHUP1_ARATH Required for the positioning and movement of chloroplasts. Interacts with profilin and actin independent of its polymerization status. Regulates chloroplast localization by anchoring chloroplasts to the plasma membrane and forming a bridge to the actin cytoskeleton.[1] [2] [3] [4]

References

  1. Kasahara M, Kagawa T, Oikawa K, Suetsugu N, Miyao M, Wada M. Chloroplast avoidance movement reduces photodamage in plants. Nature. 2002 Dec 19-26;420(6917):829-32. PMID:12490952 doi:10.1038/nature01213
  2. Oikawa K, Kasahara M, Kiyosue T, Kagawa T, Suetsugu N, Takahashi F, Kanegae T, Niwa Y, Kadota A, Wada M. Chloroplast unusual positioning1 is essential for proper chloroplast positioning. Plant Cell. 2003 Dec;15(12):2805-15. PMID:14615600 doi:10.1105/tpc.016428
  3. Schmidt von Braun S, Schleiff E. The chloroplast outer membrane protein CHUP1 interacts with actin and profilin. Planta. 2008 Apr;227(5):1151-9. PMID:18193273 doi:10.1007/s00425-007-0688-7
  4. Oikawa K, Yamasato A, Kong SG, Kasahara M, Nakai M, Takahashi F, Ogura Y, Kagawa T, Wada M. Chloroplast outer envelope protein CHUP1 is essential for chloroplast anchorage to the plasma membrane and chloroplast movement. Plant Physiol. 2008 Oct;148(2):829-42. PMID:18715957 doi:10.1104/pp.108.123075

8waf, resolution 2.80Å

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