View source for 1x91


==Crystal structure of mutant form A of a pectin methylesterase inhibitor from Arabidopsis==
<StructureSection load='1x91' size='340' side='right'caption='[[1x91]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1x91]] is a 1 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=1X91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X91 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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=1x91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x91 OCA], [https://pdbe.org/1x91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x91 RCSB], [https://www.ebi.ac.uk/pdbsum/1x91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x91 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PMEI1_ARATH PMEI1_ARATH] Inhibits pectin methylesterase from flowers and siliques.<ref>PMID:14675772</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/x9/1x91_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1x91 ConSurf].
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== Publication Abstract from PubMed ==
Pectin methylesterase (PME) and invertase are key enzymes in plant carbohydrate metabolism. Inhibitors of both enzymes constitute a sequence family of extracellular proteins. Members of this family are selectively targeted toward either PME or invertase. In a comparative structural approach we have studied how this target specificity is implemented on homologous sequences. By extending crystallographic work on the invertase inhibitor Nt-CIF to a pectin methylesterase inhibitor (PMEI) from Arabidopsis thaliana, we show an alpha-helical hairpin motif to be an independent and mobile structural entity in PMEI. Removal of this hairpin fully inactivates the inhibitor. A chimera composed of the alpha-hairpin of PMEI and the four-helix bundle of Nt-CIF is still active against PME. By contrast, combining the corresponding segment of Nt-CIF with the four-helix bundle of PMEI renders the protein inactive toward either PME or invertase. Our experiments provide insight in how these homologous inhibitors can make differential use of similar structural modules to achieve distinct functions. Integrating our results with previous findings, we present a model for the PME-PMEI complex with important implications.

Structural insights into the target specificity of plant invertase and pectin methylesterase inhibitory proteins.,Hothorn M, Wolf S, Aloy P, Greiner S, Scheffzek K Plant Cell. 2004 Dec;16(12):3437-47. Epub 2004 Nov 4. PMID:15528298<ref>PMID:15528298</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Aloy P]]
[[Category: Greiner S]]
[[Category: Hothorn M]]
[[Category: Scheffzek K]]
[[Category: Wolf S]]