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[[Image:1fm4.gif|left|200px]]<br /><applet load="1fm4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fm4, resolution 1.97&Aring;" />
'''CRYSTAL STRUCTURE OF THE BIRCH POLLEN ALLERGEN BET V 1L'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE BIRCH POLLEN ALLERGEN BET V 1L==
Bet v 1l is a naturally occurring hypoallergenic isoform of the major birch pollen allergen Bet v 1. The Bet v 1 protein belongs to the ubiquitous family of pathogenesis-related plant proteins (PR-10), which are produced in defense-response to various pathogens. Although the allergenic properties of PR-10 proteins have been extensively studied, their biological function in plants is not known. The crystal structure of Bet v 1l in complex with deoxycholate has been determined to a resolution of 1.9A using the method of molecular replacement. The structure reveals a large hydrophobic Y-shaped cavity that spans the protein and is partly occupied by two deoxycholate molecules which are bound in tandem and only partially exposed to solvent. This finding indicates that the hydrophobic cavity may have a role in facilitating the transfer of apolar ligands. The structural similarity of deoxycholate and brassinosteroids (BRs) ubiquitous plant steroid hormones, prompted the mass spectrometry (MS) study in order to examine whether BRs can bind to Bet v 1l. The MS analysis of a mixture of Bet v 1l and BRs revealed a specific non-covalent interaction of Bet v 1l with brassinolide and 24-epicastasterone. Together, our findings are consistent with a general plant-steroid carrier function for Bet v 1 and related PR-10 proteins. The role of BRs transport in PR-10 proteins may be of crucial importance in the plant defense response to pathological situations as well as in growth and development.
<StructureSection load='1fm4' size='340' side='right'caption='[[1fm4]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1fm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Betula_pendula Betula pendula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FM4 FirstGlance]. <br>
1FM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Betula_pendula Betula pendula] with <scene name='pdbligand=DXC:'>DXC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FM4 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DXC:(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC+ACID'>DXC</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fm4 OCA], [https://pdbe.org/1fm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fm4 RCSB], [https://www.ebi.ac.uk/pdbsum/1fm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fm4 ProSAT]</span></td></tr>
Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier., Markovic-Housley Z, Degano M, Lamba D, von Roepenack-Lahaye E, Clemens S, Susani M, Ferreira F, Scheiner O, Breiteneder H, J Mol Biol. 2003 Jan 3;325(1):123-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12473456 12473456]
</table>
== Function ==
[https://www.uniprot.org/uniprot/BEV1L_BETPN BEV1L_BETPN] May be a general steroid carrier protein.<ref>PMID:12473456</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fm4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <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/main_output.php?pdb_ID=1fm4 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Betula pendula]]
[[Category: Betula pendula]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Breiteneder, H.]]
[[Category: Breiteneder H]]
[[Category: Clemens, S.]]
[[Category: Clemens S]]
[[Category: Degano, M.]]
[[Category: Degano M]]
[[Category: Ferreira, F.]]
[[Category: Ferreira F]]
[[Category: Lamba, D.]]
[[Category: Lamba D]]
[[Category: Markovic-Housley, Z.]]
[[Category: Markovic-Housley Z]]
[[Category: Roepenack-Lahaye, E von.]]
[[Category: Scheiner O]]
[[Category: Scheiner, O.]]
[[Category: Susani M]]
[[Category: Susani, M.]]
[[Category: Von Roepenack-Lahaye E]]
[[Category: DXC]]
[[Category: alpha-beta: 6 anti-parallel beta strands and 3 alpha helices.]]
 
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Retrieved from "https://proteopedia.org/1fm4"