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==Crystal structure of LS24, A Seed Albumin from Lathyrus sativus==
==Crystal structure of LS24, A Seed Albumin from Lathyrus sativus==
<StructureSection load='3lp9' size='340' side='right' caption='[[3lp9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3lp9' size='340' side='right'caption='[[3lp9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3lp9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lathyrus_sativus Lathyrus sativus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LP9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LP9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3lp9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lathyrus_sativus Lathyrus sativus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LP9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</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]] 2.2&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></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=3lp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lp9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lp9 RCSB], [http://www.ebi.ac.uk/pdbsum/3lp9 PDBsum]</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=3lp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lp9 OCA], [https://pdbe.org/3lp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lp9 RCSB], [https://www.ebi.ac.uk/pdbsum/3lp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lp9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALB2_LATSA ALB2_LATSA] May play a role in response to oxidative stress and polyamine biosynthesis. The monomeric form binds one hemin per monomer. In the dimeric form, about half of the dimers bind one molecule of spermine each under physiological conditions. Ligand binding is mutually exclusive as binding of hemin leads to dissociation of the dimer.<ref>PMID:20147493</ref>
== 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/lp/3lp9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/3lp9_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=3lp9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A regulatory protein from grass pea (Lathyrus sativus), LS-24, a close homolog of albumin 2 from garden pea (Pisum sativum) that is associated with polyamine biosynthesis, was characterized and the structure of a hemopexin-type fold among plant proteins illustrated. Crystal structure of LS-24 determined at 2.2 A resolution by multiple isomorphous replacement phasing showed four-bladed beta-propeller structure having a pseudo 4-fold molecular symmetry along a metal ion-binding central channel. The structure represents typical mammalian hemopexin fold with discernible features correlated with the possible functional variations. The protein was found to exist in the dimeric state. While LS-24 dimer binds to spermine in the crystal structure as well as in solution, binding of heme in solution resulted in the dissociation of the dimer into monomers with concomitant release of bound spermine. Interactions of heme and spermine with LS-24 bear physiological implications. While binding of spermine to LS-24 can be linked with polyamine biosynthesis that of heme correlates with oxidative stress. Mutually exclusive binding of heme and spermine in different oligomeric states suggest a role for LS-24 in sensing oxidative stress through a ligand-regulated monomer-dimer transition switch.
Crystal structure and functional insights of hemopexin fold protein from grass pea.,Gaur V, Qureshi IA, Singh A, Chanana V, Salunke DM Plant Physiol. 2010 Apr;152(4):1842-50. Epub 2010 Feb 10. PMID:20147493<ref>PMID:20147493</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Albumin|Albumin]]
*[[Albumin 3D structures|Albumin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Lathyrus sativus]]
[[Category: Lathyrus sativus]]
[[Category: Chanana, V]]
[[Category: Chanana V]]
[[Category: Gaur, V]]
[[Category: Gaur V]]
[[Category: Qureshi, I A]]
[[Category: Qureshi IA]]
[[Category: Salunke, D M]]
[[Category: Salunke DM]]
[[Category: Singh, A]]
[[Category: Singh A]]
[[Category: Plant protein]]
[[Category: Seed albumin]]
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