1X32
Three Dimensional Solution Structure of the Chromo1 domain of cpSRP43
Summary for 1X32
| Entry DOI | 10.2210/pdb1x32/pdb |
| NMR Information | BMRB: 6589 |
| Descriptor | chloroplast signal recognition particle component (1 entity in total) |
| Functional Keywords | signal recognition particle, cpsrp43, chromo domain 1, lhcp, thylakoid, signaling protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Cellular location | Plastid, chloroplast stroma: O22265 |
| Total number of polymer chains | 1 |
| Total formula weight | 5048.51 |
| Authors | Sivaraja, V.,Kumar, T.K.,Henry, R.,Yu, C. (deposition date: 2005-04-28, release date: 2005-09-20, Last modification date: 2024-05-29) |
| Primary citation | Sivaraja, V.,Kumar, T.K.,Leena, P.S.,Chang, A.N.,Vidya, C.,Goforth, R.L.,Rajalingam, D.,Arvind, K.,Ye, J.L.,Chou, J.,Henry, R.,Yu, C. Three-dimensional solution structures of the chromodomains of cpSRP43 J.Biol.Chem., 280:41465-41471, 2005 Cited by PubMed Abstract: 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. PubMed: 16183644DOI: 10.1074/jbc.M507077200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
