5E4X
Crystal structure of cpSRP43 chromodomain 3
Summary for 5E4X
| Entry DOI | 10.2210/pdb5e4x/pdb |
| Descriptor | Signal recognition particle 43 kDa protein, chloroplastic, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | signal recognition particle, cpsrp43, chromodomain 3, chloroplast, transport protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Plastid, chloroplast stroma : O22265 |
| Total number of polymer chains | 1 |
| Total formula weight | 5705.56 |
| Authors | Horn, A.,Ahmed, Y.L.,Wild, K.,Sinning, I. (deposition date: 2015-10-07, release date: 2015-12-02, Last modification date: 2024-01-10) |
| Primary citation | Horn, A.,Hennig, J.,Ahmed, Y.L.,Stier, G.,Wild, K.,Sattler, M.,Sinning, I. Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction. Nat Commun, 6:8875-8875, 2015 Cited by PubMed Abstract: Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains. PubMed: 26568381DOI: 10.1038/ncomms9875 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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