1bhe: Difference between revisions
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<StructureSection load='1bhe' size='340' side='right' caption='[[1bhe]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1bhe' size='340' side='right' caption='[[1bhe]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bhe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1bhe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwinia_carotovora_carotovora Erwinia carotovora carotovora]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BHE FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=1bhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bhe RCSB], [http://www.ebi.ac.uk/pdbsum/1bhe PDBsum]</span></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=1bhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhe OCA], [http://pdbe.org/1bhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bhe RCSB], [http://www.ebi.ac.uk/pdbsum/1bhe PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PGLR2_PECSS PGLR2_PECSS]] Involved in maceration and soft-rotting of plant tissue.<ref>PMID:2215212</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1bhe" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Erwinia carotovora carotovora]] | ||
[[Category: Polygalacturonase]] | [[Category: Polygalacturonase]] | ||
[[Category: Jenkins, J]] | [[Category: Jenkins, J]] | ||
Revision as of 12:11, 10 September 2015
POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORAPOLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA
Structural highlights
Function[PGLR2_PECSS] Involved in maceration and soft-rotting of plant tissue.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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