|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal structure of BRL1 (LRR) in complex with brassinolide== | | ==Crystal structure of BRL1 (LRR) in complex with brassinolide== |
| - | <StructureSection load='4j0m' size='340' side='right' caption='[[4j0m]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4j0m' size='340' side='right'caption='[[4j0m]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j0m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J0M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j0m]] is a 2 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=4J0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J0M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BLD:BRASSINOLIDE'>BLD</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRL1, At1g55610, F20N2.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLD:BRASSINOLIDE'>BLD</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=4j0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j0m OCA], [https://pdbe.org/4j0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j0m RCSB], [https://www.ebi.ac.uk/pdbsum/4j0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j0m 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=4j0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j0m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j0m RCSB], [http://www.ebi.ac.uk/pdbsum/4j0m PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BRL1_ARATH BRL1_ARATH] Receptor with a serine/threonine-protein kinase activity. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development. Binds brassinolide. May be involved in cell growth and vascular differentiation.<ref>PMID:15486337</ref> <ref>PMID:15469497</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 16: |
Line 18: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4j0m" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 21: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Arabidopsis thaliana]] | | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Non-specific serine/threonine protein kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Chai, J]] | + | [[Category: Chai J]] |
| - | [[Category: Han, Z]] | + | [[Category: Han Z]] |
| - | [[Category: She, J]] | + | [[Category: She J]] |
| - | [[Category: Zhou, B]] | + | [[Category: Zhou B]] |
| - | [[Category: Leucine-rich repeat]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
BRL1_ARATH Receptor with a serine/threonine-protein kinase activity. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development. Binds brassinolide. May be involved in cell growth and vascular differentiation.[1] [2]
Publication Abstract from PubMed
Brassinosteroids, a group of plant steroid hormones, regulate many aspects of plant growth and development. We and other have previously solved the crystal structures of BRI1(LRR) in complex with brassinolide, the most active brassinosteroid identified thus far. Although these studies provide a structural basis for the recognition of brassinolide by its receptor BRI1, it still remains poorly understood how the hormone differentiates among its conserved receptors. Here we present the crystal structure of the BRI1 homolog BRL1 in complex with brassinolide. The structure shows that subtle differences around the brassinolide binding site can generate a striking effect on its recognition by the BRI1 family of receptors. Structural comparison of BRL1 and BRI1 in their brassinolide-bound forms reveals the molecular basis for differential binding of brassinolide to its different receptors, which can be used for more efficient design of plant growth regulators for agricultural practice. On the basis of our structural studies and others' data, we also suggest possible mechanisms for the activation of BRI1 family receptors.
Structural basis for differential recognition of brassinolide by its receptors.,She J, Han Z, Zhou B, Chai J Protein Cell. 2013 Jun;4(6):475-82. doi: 10.1007/s13238-013-3027-8. Epub 2013 May, 25. PMID:23709366[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cano-Delgado A, Yin Y, Yu C, Vafeados D, Mora-Garcia S, Cheng JC, Nam KH, Li J, Chory J. BRL1 and BRL3 are novel brassinosteroid receptors that function in vascular differentiation in Arabidopsis. Development. 2004 Nov;131(21):5341-51. PMID:15486337 doi:http://dx.doi.org/10.1242/dev.01403
- ↑ Zhou A, Wang H, Walker JC, Li J. BRL1, a leucine-rich repeat receptor-like protein kinase, is functionally redundant with BRI1 in regulating Arabidopsis brassinosteroid signaling. Plant J. 2004 Nov;40(3):399-409. PMID:15469497 doi:http://dx.doi.org/TPJ2214
- ↑ She J, Han Z, Zhou B, Chai J. Structural basis for differential recognition of brassinolide by its receptors. Protein Cell. 2013 Jun;4(6):475-82. doi: 10.1007/s13238-013-3027-8. Epub 2013 May, 25. PMID:23709366 doi:10.1007/s13238-013-3027-8
|
