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==Crystal structure of the ANX1 ectodomain from Arabidopsis thaliana== | |||
<StructureSection load='6fig' size='340' side='right' caption='[[6fig]], [[Resolution|resolution]] 1.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fig]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FIG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fig OCA], [http://pdbe.org/6fig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fig RCSB], [http://www.ebi.ac.uk/pdbsum/6fig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fig ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ANX1_ARATH ANX1_ARATH]] Receptor-like protein kinase that controls pollen tube behavior by directing rupture at proper timing to release the sperm cell.<ref>PMID:19646876</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Complex cell-to-cell communication between the male pollen tube and the female reproductive organs is required for plant fertilization. A family of Catharanthus roseus receptor kinase 1-like (CrRLK1L) membrane receptors has been genetically implicated in this process. Here, crystal structures of the CrRLK1Ls ANXUR1 and ANXUR2 are reported at 1.48 and 1.1 A resolution, respectively. The structures reveal a novel arrangement of two malectin-like domains connected by a short beta-hairpin linker and stabilized by calcium ions. The canonical carbohydrate-interaction surfaces of related animal and bacterial carbohydrate-binding modules are not conserved in plant CrRLK1Ls. In line with this, the binding of chemically diverse oligosaccharides to ANXUR1 and HERCULES1 could not be detected. Instead, CrRLK1Ls have evolved a protein-protein interface between their malectin domains which forms a deep cleft lined by highly conserved aromatic and polar residues. Analysis of the glycosylation patterns of different CrRLK1Ls and their oligomeric states suggests that this cleft could resemble a binding site for a ligand required for receptor activation of CrRLK1Ls. | |||
Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction.,Moussu S, Augustin S, Roman AO, Broyart C, Santiago J Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):671-680. doi:, 10.1107/S205979831800774X. Epub 2018 Jun 27. PMID:29968676<ref>PMID:29968676</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fig" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Non-specific serine/threonine protein kinase]] | |||
[[Category: Santiago, J]] | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Malectin-like domain]] | |||
[[Category: Membrane protein]] | |||
[[Category: Plant protein]] | |||
[[Category: Receptor kinase]] | |||
Latest revision as of 08:46, 11 July 2018
Crystal structure of the ANX1 ectodomain from Arabidopsis thalianaCrystal structure of the ANX1 ectodomain from Arabidopsis thaliana
Structural highlights
Function[ANX1_ARATH] Receptor-like protein kinase that controls pollen tube behavior by directing rupture at proper timing to release the sperm cell.[1] Publication Abstract from PubMedComplex cell-to-cell communication between the male pollen tube and the female reproductive organs is required for plant fertilization. A family of Catharanthus roseus receptor kinase 1-like (CrRLK1L) membrane receptors has been genetically implicated in this process. Here, crystal structures of the CrRLK1Ls ANXUR1 and ANXUR2 are reported at 1.48 and 1.1 A resolution, respectively. The structures reveal a novel arrangement of two malectin-like domains connected by a short beta-hairpin linker and stabilized by calcium ions. The canonical carbohydrate-interaction surfaces of related animal and bacterial carbohydrate-binding modules are not conserved in plant CrRLK1Ls. In line with this, the binding of chemically diverse oligosaccharides to ANXUR1 and HERCULES1 could not be detected. Instead, CrRLK1Ls have evolved a protein-protein interface between their malectin domains which forms a deep cleft lined by highly conserved aromatic and polar residues. Analysis of the glycosylation patterns of different CrRLK1Ls and their oligomeric states suggests that this cleft could resemble a binding site for a ligand required for receptor activation of CrRLK1Ls. Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction.,Moussu S, Augustin S, Roman AO, Broyart C, Santiago J Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):671-680. doi:, 10.1107/S205979831800774X. Epub 2018 Jun 27. PMID:29968676[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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