5y92
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana== | |
| + | <StructureSection load='5y92' size='340' side='right' caption='[[5y92]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5y92]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y92 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=5y92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y92 OCA], [http://pdbe.org/5y92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y92 RCSB], [http://www.ebi.ac.uk/pdbsum/5y92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y92 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ANX2_ARATH ANX2_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 == | ||
| + | Catharanthus roseus Receptor-Like Kinase 1-like (CrRLK1L) proteins contain two tandem malectin-like modules in their extracellular domains (ECDs) and function in diverse signaling pathways in plants. Malectin is a carbohydrate-binding protein in animals and recognizes a number of diglucosides; however, it remains unclear how the two malectin-like domains in the CrRLK1L proteins sense the ligand molecule. In this study, we reveal the crystal structures of the ECDs of ANXUR1 and ANXUR2, two CrRLK1L members in Arabidopsis thaliana that have critical functions in controlling pollen tube rupture during the fertilization process. We show that the two malectin-like domains in these proteins pack together to form a rigid architecture. Unlike animal malectin, these malectin-like domains lack residues involved in binding to the diglucosides, suggesting that they have a distinct ligand-binding mechanism. A cleft is observed between the two malectin-like domains, which might function as a potential ligand-binding pocket. This article is protected by copyright. All rights reserved. | ||
| - | + | Crystal structures of the extracellular domains of the CrRLK1L receptor-like kinases ANXUR1 and ANXUR2.,Du S, Qu LJ, Xiao J Protein Sci. 2018 Feb 1. doi: 10.1002/pro.3381. PMID:29388293<ref>PMID:29388293</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5y92" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Du, S]] | [[Category: Du, S]] | ||
| - | [[Category: Xiao, J | + | [[Category: Xiao, J Y]] |
| + | [[Category: Receptor-like kinase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:27, 28 February 2018
Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana
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