1x32
From Proteopedia
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| - | [[Image:1x32.gif|left|200px]] | + | [[Image:1x32.gif|left|200px]] |
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| - | '''Three Dimensional Solution Structure of the Chromo1 domain of cpSRP43''' | + | {{Structure |
| + | |PDB= 1x32 |SIZE=350|CAPTION= <scene name='initialview01'>1x32</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Three Dimensional Solution Structure of the Chromo1 domain of cpSRP43''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1X32 is a [ | + | 1X32 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X32 OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional solution structures of the chromodomains of cpSRP43., Sivaraja V, Kumar TK, Leena PS, Chang AN, Vidya C, Goforth RL, Rajalingam D, Arvind K, Ye JL, Chou J, Henry R, Yu C, J Biol Chem. 2005 Dec 16;280(50):41465-71. Epub 2005 Sep 23. PMID:[http:// | + | Three-dimensional solution structures of the chromodomains of cpSRP43., Sivaraja V, Kumar TK, Leena PS, Chang AN, Vidya C, Goforth RL, Rajalingam D, Arvind K, Ye JL, Chou J, Henry R, Yu C, J Biol Chem. 2005 Dec 16;280(50):41465-71. Epub 2005 Sep 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16183644 16183644] |
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thylakoid]] | [[Category: thylakoid]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:04:34 2008'' |
Revision as of 13:04, 20 March 2008
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Three Dimensional Solution Structure of the Chromo1 domain of cpSRP43
Overview
Chloroplasts contain a unique signal recognition particle (cpSRP). Unlike the cytoplasmic forms, the cpSRP lacks RNA but contains a conserved 54-kDa GTPase and a novel 43-kDa subunit (cpSRP43). Recently, three functionally distinct chromodomains (CDs) have been identified in cpSRP43. In the present study, we report the three-dimensional solution structures of the three CDs (CD1, CD2, and CD3) using a variety of triple resonance NMR experiments. The structure of CD1 consists of a triple-stranded beta-sheet segment. The C-terminal helical segment typically found in the nuclear chromodomains is absent in CD1. The secondary structural elements in CD2 and CD3 include a triple-stranded antiparallel beta-sheet and a C-terminal helix. Interestingly, the orientation of the C-terminal helix is significantly different in the structures of CD2 and CD3. Critical comparison of the structures of the chromodomains of cpSRP43 with those found in nuclear chromodomain proteins revealed that the diverse protein-protein interactions mediated by the CDs appear to stem from the differences that exist in the surface charge potentials of each CD. Results of isothermal titration calorimetry experiments confirmed that only CD2 is involved in binding to cpSRP54. The negatively charged C-terminal helix in CD2 possibly plays a crucial role in the cpSRP54-cpSRP43 interaction.
About this Structure
1X32 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structures of the chromodomains of cpSRP43., Sivaraja V, Kumar TK, Leena PS, Chang AN, Vidya C, Goforth RL, Rajalingam D, Arvind K, Ye JL, Chou J, Henry R, Yu C, J Biol Chem. 2005 Dec 16;280(50):41465-71. Epub 2005 Sep 23. PMID:16183644
Page seeded by OCA on Thu Mar 20 15:04:34 2008
