View source for 9vrc


==Cryo-EM structure of Oryza sativa multidrug resistance protein 5 (MRP5)==
<StructureSection load='9vrc' size='340' side='right'caption='[[9vrc]], [[Resolution|resolution]] 3.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vrc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VRC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.21&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9vrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vrc OCA], [https://pdbe.org/9vrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vrc RCSB], [https://www.ebi.ac.uk/pdbsum/9vrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vrc ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Phytate (phytic acid, or InsP6), the primary phosphorus storage compound in plants, plays essential roles in nutrient homeostasis and cellular signaling. However, its strong metal-chelating properties make cytosolic accumulation cytotoxic, necessitating its sequestration into vacuoles for safe storage. Here, we present the cryo-EM structures of the rice vacuolar phytate transporter, OsMRP5, captured in distinct functional states. These structures reveal the molecular basis of OsMRP5 function as an ATP-binding cassette (ABC) transporter. OsMRP5 employs a specialized substrate-recognition mechanism, uniquely adapted to bind the fully hydrophilic InsP6 through extensive electrostatic and hydrogen-bonding interactions within two distinct, highly polar binding sites in its central cavity. A distinctive electropositive tunnel, positioned above the central cavity, forms a continuous pathway connecting the InsP6-binding pocket to the vacuolar export site. This tunnel likely generates an electrostatic attraction that facilitates the movement of the highly anionic InsP6 through the transporter. By mapping mutations from low-phytic acid (lpa) crop variants onto the OsMRP5 structures, we pinpoint their conserved locations critical for transporter function and validate their impact experimentally. These results reveal how OsMRP5 recognizes and transports the highly charged InsP6 molecule into vacuoles, providing a molecular framework for targeted manipulation of this agriculturally important transporter.

Cryo-EM structures of Oryza sativa MRP5 reveal a phytate accumulation mechanism in plant vacuoles.,Zuo J, Zhang J, Tang Y, Jiang L, Cao S, Liu Y, Shen C, Wang C, Chen H, Xiong L, Yin P, Gong Z, Liu Z Plant Cell. 2026 Mar 24:koag088. doi: 10.1093/plcell/koag088. PMID:41875395<ref>PMID:41875395</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Oryza sativa Japonica Group]]
[[Category: Liu Z]]
[[Category: Zhang J]]
[[Category: Zou J]]