5gui

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Crystal structure of the N-terminal Domain of Caseinolytic protease associated chaperone ClpC1 from Arabidopsis thalianaCrystal structure of the N-terminal Domain of Caseinolytic protease associated chaperone ClpC1 from Arabidopsis thaliana

Structural highlights

5gui is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CLPC1_ARATH] Molecular chaperone that hydrolyzes ATP and is associated with the chloroplast protein import apparatus. May function as the motor for chloroplast protein translocation, as translocation requires ATP hydrolysis in the stroma. May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast. Involved in the regulation of chlorophyll b biosynthesis through the destabilization of chlorophyllide a oxygenase (CAO) protein in response to the accumulation of chlorophyll b. Involved in leaf iron homeostasis.[1] [2] [3] [4] [5] [6] [7] [8]

References

  1. ↑ Park S, Rodermel SR. Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid membrane biogenesis. Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12765-70. Epub 2004 Aug 10. PMID:15304652 doi:http://dx.doi.org/10.1073/pnas.0402764101
  2. ↑ Constan D, Froehlich JE, Rangarajan S, Keegstra K. A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis. Plant Physiol. 2004 Nov;136(3):3605-15. Epub 2004 Oct 29. PMID:15516497 doi:http://dx.doi.org/10.1104/pp.104.052928
  3. ↑ Kovacheva S, Bedard J, Patel R, Dudley P, Twell D, Rios G, Koncz C, Jarvis P. In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import. Plant J. 2005 Feb;41(3):412-28. PMID:15659100 doi:http://dx.doi.org/10.1111/j.1365-313X.2004.02307.x
  4. ↑ Nakagawara E, Sakuraba Y, Yamasato A, Tanaka R, Tanaka A. Clp protease controls chlorophyll b synthesis by regulating the level of chlorophyllide a oxygenase. Plant J. 2007 Mar;49(5):800-9. Epub 2007 Feb 9. PMID:17291312 doi:http://dx.doi.org/10.1111/j.1365-313X.2006.02996.x
  5. ↑ Kovacheva S, Bedard J, Wardle A, Patel R, Jarvis P. Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import. Plant J. 2007 Apr;50(2):364-79. Epub 2007 Mar 21. PMID:17376159 doi:http://dx.doi.org/10.1111/j.1365-313X.2007.03060.x
  6. ↑ Wu H, Ji Y, Du J, Kong D, Liang H, Ling HQ. ClpC1, an ATP-dependent Clp protease in plastids, is involved in iron homeostasis in Arabidopsis leaves. Ann Bot. 2010 May;105(5):823-33. doi: 10.1093/aob/mcq051. Epub 2010 Apr 9. PMID:20382967 doi:http://dx.doi.org/10.1093/aob/mcq051
  7. ↑ Chu CC, Li HM. The amino-terminal domain of chloroplast Hsp93 is important for its membrane association and functions in vivo. Plant Physiol. 2012 Apr;158(4):1656-65. doi: 10.1104/pp.112.193300. Epub 2012 Feb, 21. PMID:22353577 doi:http://dx.doi.org/10.1104/pp.112.193300
  8. ↑ Sjogren LL, Tanabe N, Lymperopoulos P, Khan NZ, Rodermel SR, Aronsson H, Clarke AK. Quantitative analysis of the chloroplast molecular chaperone ClpC/Hsp93 in Arabidopsis reveals new insights into its localization, interaction with the Clp proteolytic core, and functional importance. J Biol Chem. 2014 Apr 18;289(16):11318-30. doi: 10.1074/jbc.M113.534552. Epub, 2014 Mar 5. PMID:24599948 doi:http://dx.doi.org/10.1074/jbc.M113.534552

5gui, resolution 1.20Å

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