5y92: Difference between revisions

Latest revision as of 10:58, 30 October 2024

Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana

Structural highlights

5y92 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.004Å
Ligands:	BMA, NAG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANX2_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 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^[2]

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

References

↑ Miyazaki S, Murata T, Sakurai-Ozato N, Kubo M, Demura T, Fukuda H, Hasebe M. ANXUR1 and 2, sister genes to FERONIA/SIRENE, are male factors for coordinated fertilization. Curr Biol. 2009 Aug 11;19(15):1327-31. doi: 10.1016/j.cub.2009.06.064. Epub 2009 , Jul 30. PMID:19646876 doi:https://dx.doi.org/10.1016/j.cub.2009.06.064
↑ Du S, Qu LJ, Xiao J. Crystal structures of the extracellular domains of the CrRLK1L receptor-like kinases ANXUR1 and ANXUR2. Protein Sci. 2018 Feb 1. doi: 10.1002/pro.3381. PMID:29388293 doi:https://dx.doi.org/10.1002/pro.3381

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Miyazaki S, Murata T, Sakurai-Ozato N, Kubo M, Demura T, Fukuda H, Hasebe M. ANXUR1 and 2, sister genes to FERONIA/SIRENE, are male factors for coordinated fertilization. Curr Biol. 2009 Aug 11;19(15):1327-31. doi: 10.1016/j.cub.2009.06.064. Epub 2009 , Jul 30. PMID:19646876 doi:https://dx.doi.org/10.1016/j.cub.2009.06.064

[2] Du S, Qu LJ, Xiao J. Crystal structures of the extracellular domains of the CrRLK1L receptor-like kinases ANXUR1 and ANXUR2. Protein Sci. 2018 Feb 1. doi: 10.1002/pro.3381. PMID:29388293 doi:https://dx.doi.org/10.1002/pro.3381

[1]

[2]

@@ Line 1: / Line 1: @@
 ==Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana==
-<StructureSection load='5y92' size='340' side='right' caption='[[5y92]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='5y92' size='340' side='right'caption='[[5y92]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5y92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. 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>
+<table><tr><td colspan='2'>[[5y92]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.004&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANX2, At5g28680, F4I4.60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5y92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y92 OCA], [https://pdbe.org/5y92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y92 RCSB], [https://www.ebi.ac.uk/pdbsum/5y92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y92 ProSAT]</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>
+[https://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 ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Non-specific serine/threonine protein kinase]]
+[[Category: Large Structures]]
-[[Category: Du, S]]
+[[Category: Du S]]
-[[Category: Xiao, J Y]]
+[[Category: Xiao JY]]
-[[Category: Receptor-like kinase]]
-[[Category: Transferase]]

5y92: Difference between revisions

Latest revision as of 10:58, 30 October 2024

Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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