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New page: left|200px<br /><applet load="1bhe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhe, resolution 1.9Å" /> '''POLYGALACTURONASE FRO...
 
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[[Image:1bhe.gif|left|200px]]<br /><applet load="1bhe" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bhe, resolution 1.9&Aring;" />
'''POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA'''<br />


==Overview==
==POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA==
The crystal structure of the 40-kDa endo-polygalacturonase from Erwinia, carotovora ssp. carotovora was solved by multiple isomorphous replacement, and refined at 1.9 A to a conventional crystallographic R-factor of 0.198, and Rfree of 0.239. This is the first structure of a polygalacturonase and, comprises a 10 turn right-handed parallel beta-helix domain with two loop, regions forming a "tunnel like" substrate-binding cleft. Sequence, conservation indicates that the active site of polygalacturonase is, between these two loop regions, and comparison of the structure of, polygalacturonase with that of rhamnogalacturonase A from Aspergillus, aculeatus enables two conserved aspartates, presumed to be catalytic, residues, to be identified. An adjacent histidine, in accord with, biochemical results, is also seen. A similarity in overall electrostatic, properties of the substrate-binding clefts of polygalacturonase and, pectate lyase, which bind and cleave the same substrate, polygalacturonic, acid, is also revealed.
<StructureSection load='1bhe' size='340' side='right'caption='[[1bhe]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bhe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum_subsp._carotovorum Pectobacterium carotovorum subsp. carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHE 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]] 1.9&#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=1bhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhe OCA], [https://pdbe.org/1bhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bhe RCSB], [https://www.ebi.ac.uk/pdbsum/1bhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bhe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PGLR2_PECPM PGLR2_PECPM] Involved in maceration and soft-rotting of plant tissue.<ref>PMID:2215212</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/bh/1bhe_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=1bhe ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the 40-kDa endo-polygalacturonase from Erwinia carotovora ssp. carotovora was solved by multiple isomorphous replacement and refined at 1.9 A to a conventional crystallographic R-factor of 0.198 and Rfree of 0.239. This is the first structure of a polygalacturonase and comprises a 10 turn right-handed parallel beta-helix domain with two loop regions forming a "tunnel like" substrate-binding cleft. Sequence conservation indicates that the active site of polygalacturonase is between these two loop regions, and comparison of the structure of polygalacturonase with that of rhamnogalacturonase A from Aspergillus aculeatus enables two conserved aspartates, presumed to be catalytic residues, to be identified. An adjacent histidine, in accord with biochemical results, is also seen. A similarity in overall electrostatic properties of the substrate-binding clefts of polygalacturonase and pectate lyase, which bind and cleave the same substrate, polygalacturonic acid, is also revealed.


==About this Structure==
Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora.,Pickersgill R, Smith D, Worboys K, Jenkins J J Biol Chem. 1998 Sep 18;273(38):24660-4. PMID:9733763<ref>PMID:9733763</ref>
1BHE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Active as [http://en.wikipedia.org/wiki/Polygalacturonase Polygalacturonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.15 3.2.1.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BHE OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora., Pickersgill R, Smith D, Worboys K, Jenkins J, J Biol Chem. 1998 Sep 18;273(38):24660-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9733763 9733763]
</div>
[[Category: Pectobacterium carotovorum]]
<div class="pdbe-citations 1bhe" style="background-color:#fffaf0;"></div>
[[Category: Polygalacturonase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Jenkins, J.]]
__TOC__
[[Category: Pickersgill, R.]]
</StructureSection>
[[Category: Smith, D.]]
[[Category: Large Structures]]
[[Category: Worboys, K.]]
[[Category: Pectobacterium carotovorum subsp. carotovorum]]
[[Category: family 28 glycosyl hydrolase]]
[[Category: Jenkins J]]
[[Category: glycosidase]]
[[Category: Pickersgill R]]
[[Category: hydrolyses polygalacturonic acid]]
[[Category: Smith D]]
 
[[Category: Worboys K]]
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Retrieved from "https://proteopedia.org/1bhe"