1jrg

<table><tr><td colspan='2'>[[1jrg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"erwinia_carotovora_var._chrysanthemi"_(burkholder_et_al._1953)_dye_1969 "erwinia carotovora var. chrysanthemi" (burkholder et al. 1953) dye 1969]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JRG FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jta|1jta]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PELA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 "Erwinia carotovora var. chrysanthemi" (Burkholder et al. 1953) Dye 1969])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1jrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jrg OCA], [http://pdbe.org/1jrg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jrg RCSB], [http://www.ebi.ac.uk/pdbsum/1jrg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jrg ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PLYA_DICCH PLYA_DICCH]] Involved in maceration and soft-rotting of plant tissue.

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== Publication Abstract from PubMed ==

Pectate lyase A is a virulence factor secreted by the plant-pathogenic bacteria Erwinia chrysanthemi. The enzyme cleaves the glycosidic bond of pectate polymers by a calcium-dependent beta-elimination mechanism. The crystal structure of pectate lyase A from E. chrysanthemi EC16 has been determined in two crystal forms, monoclinic C2 to 1.8 A and rhombohedral R3 to 2.1 A. The protein structure is compared with two other pectate lyase isoforms from E. chrysanthemi EC16, pectate lyase C and pectate lyase E. Pectate lyase A is unique as it is the only acidic pectate lyase and has end products that are significantly more varied in length in comparison to those of the other four major pectate lyase isozymes. Differences and similarities in polypeptide trace, size and volume of the active-site groove and surface electrostatics are discussed.

Structure of pectate lyase A: comparison to other isoforms.,Thomas LM, Doan CN, Oliver RL, Yoder MD Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1008-15. Epub, 2002 May 29. PMID:12037303<ref>PMID:12037303</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jrg" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Doan, C]]

[[Category: Oliver, R L]]

[[Category: Thomas, L M]]

[[Category: Yoder, M D]]

[[Category: Parallel beta helix beta elimination]]