1bhe
From Proteopedia
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| - | [[Image:1bhe.gif|left|200px]]<br /><applet load="1bhe" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1bhe, resolution 1.9Å" /> | ||
| - | '''POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA'''<br /> | ||
| - | == | + | ==POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA== |
| + | <StructureSection load='1bhe' size='340' side='right'caption='[[1bhe]], [[Resolution|resolution]] 1.90Å' 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]] 1.9Å</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. | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1bhe" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | + | <references/> | |
| - | [[Category: Jenkins | + | __TOC__ |
| - | [[Category: Pickersgill | + | </StructureSection> |
| - | [[Category: Smith | + | [[Category: Large Structures]] |
| - | [[Category: Worboys | + | [[Category: Pectobacterium carotovorum subsp. carotovorum]] |
| - | + | [[Category: Jenkins J]] | |
| - | + | [[Category: Pickersgill R]] | |
| - | + | [[Category: Smith D]] | |
| - | + | [[Category: Worboys K]] | |
| - | + | ||
Current revision
POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA
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