5e4w | pdb_00005e4w

Crystal structure of cpSRP43 chromodomains 2 and 3 in complex with the Alb3 tail

spinqualitylabelsall models 5e4w, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e4w is a 6 chain structure with sequence from Arabidopsis thaliana and Escherichia coli O157:H7. 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: CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THIO_ECO57 Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Publication Abstract from PubMed 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. Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.,Horn A, Hennig J, Ahmed YL, Stier G, Wild K, Sattler M, Sinning I Nat Commun. 2015 Nov 16;6:8875. doi: 10.1038/ncomms9875. PMID:26568381 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Signal recognition particle 3D structures Thioredoxin 3D structures

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