5zmf

AMPPNP complex of C. reinhardtii ArsA1

spinqualitylabelsall models 5zmf, resolution 3.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zmf is a 1 chain structure with sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.556Å Ligands: ANP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ASNA1_CHLRE ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the chloroplast. Required for the accumulation of TOC34, an essential component of the outer chloroplast membrane translocon (TOC) complex (PubMed:23167510, PubMed:28382961). Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to chloroplast, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis (PubMed:28382961). Publication Abstract from PubMed Tail-anchored (TA) membrane proteins destined for the posttranslational pathway are safely delivered to the endoplasmic reticulum (ER) membrane by a well-known targeting factor, TRC40/Get3, in mammals and yeast. In contrast, the underlying mechanism for translocation of TA proteins in plants remains obscure. How this unique eukaryotic membrane-trafficking system correctly distinguishes different subsets of TA proteins destined for various organelles, including mitochondria, chloroplasts and the ER, is a key long-standing question. Here, we present crystal structures of algae ArsA1 (the Get3 homolog) in a distinct open state of nucleotide-free and AMPPNP-bound. This ~80-kDa protein possesses a monomeric architecture, with two ATPase domains in a single polypeptide chain. It is capable of binding chloroplast (TOC34 and TOC159) and mitochondrial (TOM7) TA proteins based on features of its transmembrane domain as well as the regions right before and after the transmembrane domain. Several helices located above the TA-binding groove comprise the interlocking hook-like motif implicated in TA substrate recognition by mutational analyses. Our data provide insights into the molecular basis of the highly specific selectivity of algae ArsA1 interactions with the correct sets of TA substrates before membrane targeting in plant cells. This article is protected by copyright. All rights reserved. Structural analysis of chloroplast tail-anchored membrane protein recognition by ArsA1.,Lin TW, Chen CC, Wu SM, Chang YC, Li YC, Su YW, Hsiao CD, Chang HY Plant J. 2019 Mar 20. doi: 10.1111/tpj.14316. PMID:30891827 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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