3ebl

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Revision as of 10:15, 5 August 2016

Crystal Structure of Rice GID1 complexed with GA4

Structural highlights

3ebl is a 6 chain structure with sequence from Japanese rice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Gene:	GID1, Os05g0407500, LOC_Os05g33730, OJ1657_H11.10, P0040B10.6 (Japanese rice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GID1_ORYSJ] Functions as soluble gibberellin (GA) receptor. GA is an essential hormone that regulates growth and development in plants. Binds with high affinity the biologically active GAs such as GA1, GA3 and GA4, but has low or no affinity for the biologically inactive GAs. Upon GA-binding, it interacts with the DELLA protein SLR1, a repressor of GA signaling. This leads to SLR1 degradation by the proteasome, allowing the GA signaling pathway.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Gibberellins (GAs) are phytohormones essential for many developmental processes in plants. A nuclear GA receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), has a primary structure similar to that of the hormone-sensitive lipases (HSLs). Here we analyse the crystal structure of Oryza sativa GID1 (OsGID1) bound with GA(4) and GA(3) at 1.9 A resolution. The overall structure of both complexes shows an alpha/beta-hydrolase fold similar to that of HSLs except for an amino-terminal lid. The GA-binding pocket corresponds to the substrate-binding site of HSLs. On the basis of the OsGID1 structure, we mutagenized important residues for GA binding and examined their binding activities. Almost all of them showed very little or no activity, confirming that the residues revealed by structural analysis are important for GA binding. The replacement of Ile 133 with Leu or Val-residues corresponding to those of the lycophyte Selaginella moellendorffii GID1s-caused an increase in the binding affinity for GA(34), a 2beta-hydroxylated GA(4). These observations indicate that GID1 originated from HSL and was further modified to have higher affinity and more strict selectivity for bioactive GAs by adapting the amino acids involved in GA binding in the course of plant evolution.

Structural basis for gibberellin recognition by its receptor GID1.,Shimada A, Ueguchi-Tanaka M, Nakatsu T, Nakajima M, Naoe Y, Ohmiya H, Kato H, Matsuoka M Nature. 2008 Nov 27;456(7221):520-3. doi: 10.1038/nature07546. PMID:19037316^[1]

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

References

↑ Shimada A, Ueguchi-Tanaka M, Nakatsu T, Nakajima M, Naoe Y, Ohmiya H, Kato H, Matsuoka M. Structural basis for gibberellin recognition by its receptor GID1. Nature. 2008 Nov 27;456(7221):520-3. doi: 10.1038/nature07546. PMID:19037316 doi:http://dx.doi.org/10.1038/nature07546

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ebl"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Rice GID1 complexed with GA4==
 <StructureSection load='3ebl' size='340' side='right' caption='[[3ebl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GA4:GIBBERELLIN+A4'>GA4</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GID1, Os05g0407500, LOC_Os05g33730, OJ1657_H11.10, P0040B10.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice])</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=3ebl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ebl RCSB], [http://www.ebi.ac.uk/pdbsum/3ebl PDBsum]</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=3ebl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebl OCA], [http://pdbe.org/3ebl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ebl RCSB], [http://www.ebi.ac.uk/pdbsum/3ebl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ebl ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ebl ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3ebl" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3ebl

From Proteopedia

Revision as of 10:15, 5 August 2016

Crystal Structure of Rice GID1 complexed with GA4

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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