2i9y: Difference between revisions

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==Solution structure of Arabidopsis thaliana protein At1g70830, a member of the major latex protein family==
==Solution structure of Arabidopsis thaliana protein At1g70830, a member of the major latex protein family==
<StructureSection load='2i9y' size='340' side='right' caption='[[2i9y]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2i9y' size='340' side='right'caption='[[2i9y]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2i9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I9Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[2i9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I9Y FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AT1G70830, MLP28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2i9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2i9y RCSB], [http://www.ebi.ac.uk/pdbsum/2i9y PDBsum], [http://www.topsan.org/Proteins/CESG/2i9y TOPSAN]</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=2i9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i9y OCA], [https://pdbe.org/2i9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i9y RCSB], [https://www.ebi.ac.uk/pdbsum/2i9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i9y ProSAT], [https://www.topsan.org/Proteins/CESG/2i9y TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MLP28_ARATH MLP28_ARATH]] Can bind steroids (in vitro), and may also bind other types of hydrophobic ligands.  
[https://www.uniprot.org/uniprot/MLP28_ARATH MLP28_ARATH] Can bind steroids (in vitro), and may also bind other types of hydrophobic ligands.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/2i9y_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/2i9y_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=2i9y ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The major latex proteins (MLP) are a protein family first identified in the latex of opium poppy. They are found only in plants and have 24 identified members in Arabidopsis alone as well as in other plants such as peach, strawberry, melon, cucumber, and soybean. While the function of the MLPs is unknown, they have been associated with fruit and flower development and in pathogen defense responses. Based on modest sequence similarity, they have been characterized as members of the Bet v 1 protein superfamily; however, no structures have yet been reported. As part of an ongoing structural genomics effort, we determined the structures of two Arabidopsis thaliana MLPs: the solution structure of MLP28 (gene product of At1g70830.1) and the crystal structure of At1g24000.1. The structures revealed distinct differences when compared to one another and to the typical Bet v 1 fold. Nevertheless, NMR titration experiments demonstrated that the characteristic Bet v 1 hydrophobic binding pocket of At1g24000.1 is able to bind a ligand, suggesting that it plays a role in the function of the MLPs. A structure-based sequence analysis identified conserved hydrophobic residues in the long alpha helix that contribute to the binding cavity and may specify preferred ligands for the MLP family.
Structures of two Arabidopsis thaliana major latex proteins represent novel helix-grip folds.,Lytle BL, Song J, de la Cruz NB, Peterson FC, Johnson KA, Bingman CA, Phillips GN Jr, Volkman BF Proteins. 2009 Jul;76(1):237-43. doi: 10.1002/prot.22396. PMID:19326460<ref>PMID:19326460</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2i9y" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Structural genomic]]
[[Category: Large Structures]]
[[Category: Cruz, N B.de la]]
[[Category: Lytle BL]]
[[Category: Lytle, B L]]
[[Category: Peterson FC]]
[[Category: Peterson, F C]]
[[Category: Volkman BF]]
[[Category: Volkman, B F]]
[[Category: De la Cruz NB]]
[[Category: At1g70830]]
[[Category: Bet v1-like]]
[[Category: Cesg]]
[[Category: PSI, Protein structure initiative]]
[[Category: Unknown function]]

Latest revision as of 22:03, 29 May 2024

Solution structure of Arabidopsis thaliana protein At1g70830, a member of the major latex protein familySolution structure of Arabidopsis thaliana protein At1g70830, a member of the major latex protein family

Structural highlights

2i9y is a 1 chain structure with sequence from Arabidopsis thaliana. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

MLP28_ARATH Can bind steroids (in vitro), and may also bind other types of hydrophobic ligands.

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

The major latex proteins (MLP) are a protein family first identified in the latex of opium poppy. They are found only in plants and have 24 identified members in Arabidopsis alone as well as in other plants such as peach, strawberry, melon, cucumber, and soybean. While the function of the MLPs is unknown, they have been associated with fruit and flower development and in pathogen defense responses. Based on modest sequence similarity, they have been characterized as members of the Bet v 1 protein superfamily; however, no structures have yet been reported. As part of an ongoing structural genomics effort, we determined the structures of two Arabidopsis thaliana MLPs: the solution structure of MLP28 (gene product of At1g70830.1) and the crystal structure of At1g24000.1. The structures revealed distinct differences when compared to one another and to the typical Bet v 1 fold. Nevertheless, NMR titration experiments demonstrated that the characteristic Bet v 1 hydrophobic binding pocket of At1g24000.1 is able to bind a ligand, suggesting that it plays a role in the function of the MLPs. A structure-based sequence analysis identified conserved hydrophobic residues in the long alpha helix that contribute to the binding cavity and may specify preferred ligands for the MLP family.

Structures of two Arabidopsis thaliana major latex proteins represent novel helix-grip folds.,Lytle BL, Song J, de la Cruz NB, Peterson FC, Johnson KA, Bingman CA, Phillips GN Jr, Volkman BF Proteins. 2009 Jul;76(1):237-43. doi: 10.1002/prot.22396. PMID:19326460[1]

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

References

  1. Lytle BL, Song J, de la Cruz NB, Peterson FC, Johnson KA, Bingman CA, Phillips GN Jr, Volkman BF. Structures of two Arabidopsis thaliana major latex proteins represent novel helix-grip folds. Proteins. 2009 Jul;76(1):237-43. PMID:19326460 doi:10.1002/prot.22396
Drag the structure with the mouse to rotate

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