7cjs

From Proteopedia

(Difference between revisions)

Revision as of 10:49, 16 February 2022

structure of aquaporin

Structural highlights

7cjs is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NIP21_ORYSJ] Silicon influx transporter responsible for silicon transport from the external solution to the root cells (PubMed:16572174). Is coupled with the silicon efflux transporter LSI2 in both exodermal and endodermal root cells for an efficient silicon transport across the cells into the stele (PubMed:17625566). Silicon is beneficial to plant growth and helps plants to overcome abiotic and biotic stresses by preventing lodging (falling over) and increasing resistance to pests and diseases, as well as other stresses (PubMed:16572174). Is coupled with LSI2 transporter in roots for efficient uptake of arsenite, which is further dispatched in shoots and grains (PubMed:18626020). Mediates uptake of methylated arsenic species in roots (PubMed:19542298).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Silicon (Si), the most abundant mineral element in the earth's crust, is taken up by plant roots in the form of silicic acid through Low silicon rice 1 (Lsi1). Lsi1 belongs to the Nodulin 26-like intrinsic protein subfamily in aquaporin and shows high selectivity for silicic acid. To uncover the structural basis for this high selectivity, here we show the crystal structure of the rice Lsi1 at a resolution of 1.8 A. The structure reveals transmembrane helical orientations different from other aquaporins, characterized by a unique, widely opened, and hydrophilic selectivity filter (SF) composed of five residues. Our structural, functional, and theoretical investigations provide a solid structural basis for the Si uptake mechanism in plants, which will contribute to secure and sustainable rice production by manipulating Lsi1 selectivity for different metalloids.

Structural basis for high selectivity of a rice silicon channel Lsi1.,Saitoh Y, Mitani-Ueno N, Saito K, Matsuki K, Huang S, Yang L, Yamaji N, Ishikita H, Shen JR, Ma JF, Suga M Nat Commun. 2021 Oct 29;12(1):6236. doi: 10.1038/s41467-021-26535-x. PMID:34716344^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ma JF, Tamai K, Yamaji N, Mitani N, Konishi S, Katsuhara M, Ishiguro M, Murata Y, Yano M. A silicon transporter in rice. Nature. 2006 Mar 30;440(7084):688-91. doi: 10.1038/nature04590. PMID:16572174 doi:http://dx.doi.org/10.1038/nature04590
↑ Ma JF, Yamaji N, Mitani N, Tamai K, Konishi S, Fujiwara T, Katsuhara M, Yano M. An efflux transporter of silicon in rice. Nature. 2007 Jul 12;448(7150):209-12. PMID:17625566 doi:http://dx.doi.org/nature05964
↑ Ma JF, Yamaji N, Mitani N, Xu XY, Su YH, McGrath SP, Zhao FJ. Transporters of arsenite in rice and their role in arsenic accumulation in rice grain. Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):9931-5. doi:, 10.1073/pnas.0802361105. Epub 2008 Jul 14. PMID:18626020 doi:http://dx.doi.org/10.1073/pnas.0802361105
↑ Li RY, Ago Y, Liu WJ, Mitani N, Feldmann J, McGrath SP, Ma JF, Zhao FJ. The rice aquaporin Lsi1 mediates uptake of methylated arsenic species. Plant Physiol. 2009 Aug;150(4):2071-80. doi: 10.1104/pp.109.140350. Epub 2009 Jun, 19. PMID:19542298 doi:http://dx.doi.org/10.1104/pp.109.140350
↑ Saitoh Y, Mitani-Ueno N, Saito K, Matsuki K, Huang S, Yang L, Yamaji N, Ishikita H, Shen JR, Ma JF, Suga M. Structural basis for high selectivity of a rice silicon channel Lsi1. Nat Commun. 2021 Oct 29;12(1):6236. doi: 10.1038/s41467-021-26535-x. PMID:34716344 doi:http://dx.doi.org/10.1038/s41467-021-26535-x

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7cjs"

@@ Line 1: / Line 1: @@
 ==structure of aquaporin==
-<StructureSection load='7cjs' size='340' side='right'caption='[[7cjs]]' scene=''>
+<StructureSection load='7cjs' size='340' side='right'caption='[[7cjs]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CJS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7cjs]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CJS FirstGlance]. <br>
-</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=7cjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cjs OCA], [https://pdbe.org/7cjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cjs RCSB], [https://www.ebi.ac.uk/pdbsum/7cjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cjs ProSAT]</span></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></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=7cjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cjs OCA], [https://pdbe.org/7cjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cjs RCSB], [https://www.ebi.ac.uk/pdbsum/7cjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cjs ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[https://www.uniprot.org/uniprot/NIP21_ORYSJ NIP21_ORYSJ]] Silicon influx transporter responsible for silicon transport from the external solution to the root cells (PubMed:16572174). Is coupled with the silicon efflux transporter LSI2 in both exodermal and endodermal root cells for an efficient silicon transport across the cells into the stele (PubMed:17625566). Silicon is beneficial to plant growth and helps plants to overcome abiotic and biotic stresses by preventing lodging (falling over) and increasing resistance to pests and diseases, as well as other stresses (PubMed:16572174). Is coupled with LSI2 transporter in roots for efficient uptake of arsenite, which is further dispatched in shoots and grains (PubMed:18626020). Mediates uptake of methylated arsenic species in roots (PubMed:19542298).<ref>PMID:16572174</ref> <ref>PMID:17625566</ref> <ref>PMID:18626020</ref> <ref>PMID:19542298</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Silicon (Si), the most abundant mineral element in the earth's crust, is taken up by plant roots in the form of silicic acid through Low silicon rice 1 (Lsi1). Lsi1 belongs to the Nodulin 26-like intrinsic protein subfamily in aquaporin and shows high selectivity for silicic acid. To uncover the structural basis for this high selectivity, here we show the crystal structure of the rice Lsi1 at a resolution of 1.8 A. The structure reveals transmembrane helical orientations different from other aquaporins, characterized by a unique, widely opened, and hydrophilic selectivity filter (SF) composed of five residues. Our structural, functional, and theoretical investigations provide a solid structural basis for the Si uptake mechanism in plants, which will contribute to secure and sustainable rice production by manipulating Lsi1 selectivity for different metalloids.
+Structural basis for high selectivity of a rice silicon channel Lsi1.,Saitoh Y, Mitani-Ueno N, Saito K, Matsuki K, Huang S, Yang L, Yamaji N, Ishikita H, Shen JR, Ma JF, Suga M Nat Commun. 2021 Oct 29;12(1):6236. doi: 10.1038/s41467-021-26535-x. PMID:34716344<ref>PMID:34716344</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7cjs" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Ma JF]]
+[[Category: Ma, J F]]
-[[Category: Saitoh Y]]
+[[Category: Saitoh, Y]]
-[[Category: Suga M]]
+[[Category: Suga, M]]
+[[Category: Aquaporn]]
+[[Category: Transport protein]]

7cjs

From Proteopedia

Revision as of 10:49, 16 February 2022

structure of aquaporin

Structural highlights

Function

Publication Abstract from PubMed

References

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