4tum | pdb_00004tum
Crystal structure of Ankyrin Repeat Domain of AKR2
Structural highlights
FunctionAKR2A_ARATH Exhibits chaperone activity toward chloroplast outer envelope membrane, mitochondrion outer membrane, endoplasmic reticulum membrane and peroxisomal proteins, by recruiting specific proteins containing a single transmembrane associated with an AKR2A-binding sequence (ABS) and subsequently binding glycolipids (e.g. monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG)) present in the membrane of the target organelle (PubMed:18193034, PubMed:20215589, PubMed:25203210). Seems to be involved in the regulation of hydrogen peroxide levels during biotic and abiotic stresses by optimizing the ascorbate peroxidase 3 (APX3) hydrogen peroxide-degrading activity. This regulation might be monitored by GRF6. Cytosolic targeting factor for chloroplast outer membrane (COM) proteins that mediates sorting and targeting of nascent chloroplast outer envelope membrane (OEM) proteins to the chloroplast. Facilitates the targeting of OEP7 to chloroplasts (PubMed:18193034). Facilitates the targeting of APX3 to peroxisomes. Involved in cellular metabolism (e.g. peroxisome activity) and required for plant growth and development (PubMed:20215589).[1] [2] [3] [4] Publication Abstract from PubMedIn organellogenesis of the chloroplast from endosymbiotic cyanobacteria, the establishment of protein-targeting mechanisms to the chloroplast should have been pivotal. However, it is still mysterious how these mechanisms were established and how they work in plant cells. Here we show that AKR2A, the cytosolic targeting factor for chloroplast outer membrane (COM) proteins, evolved from the ankyrin repeat domain (ARD) of the host cell by stepwise extensions of its N-terminal domain and that two lipids, monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG), of the endosymbiont were selected to function as the AKR2A receptor. Structural analysis, molecular modeling, and mutational analysis of the ARD identified two adjacent sites for coincidental and synergistic binding of MGDG and PG. Based on these findings, we propose that the targeting mechanism of COM proteins was established using components from both the endosymbiont and host cell through a modification of the protein-protein-interacting ARD into a lipid binding domain. An Ankyrin Repeat Domain of AKR2 Drives Chloroplast Targeting through Coincident Binding of Two Chloroplast Lipids.,Kim DH, Park MJ, Gwon GH, Silkov A, Xu ZY, Yang EC, Song S, Song K, Kim Y, Yoon HS, Honig B, Cho W, Cho Y, Hwang I Dev Cell. 2014 Sep 8;30(5):598-609. doi: 10.1016/j.devcel.2014.07.026. PMID:25203210[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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