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{{STRUCTURE_4hwv|  PDB=4hwv  |  SCENE=  }}
===Structure of Pectate Lyase from Acidovorax avenae subsp citrulli===
{{ABSTRACT_PUBMED_23568384}}


==About this Structure==
==Structure of Pectate Lyase from Acidovorax avenae subsp citrulli==
[[4hwv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acidovorax_citrulli_aac00-1 Acidovorax citrulli aac00-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWV OCA].  
<StructureSection load='4hwv' size='340' side='right'caption='[[4hwv]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hwv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidovorax_citrulli_AAC00-1 Acidovorax citrulli AAC00-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HWV 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]] 1.37&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4hwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwv OCA], [https://pdbe.org/4hwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hwv RCSB], [https://www.ebi.ac.uk/pdbsum/4hwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwv ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pectates lyase (Pel) plays an important role in bacteria pathogenicity. The crystal structure of Pel from Acidovorax citrulli (AcPel) has been solved to 1.37 A resolution. AcPel belongs to the polysaccharide lyase family 1 (PL1), which has a characteristic right-handed beta-helix fold. AcPel is similar with other Pels in the PL1 family, but also shows some differences at the substrate binding site.


==Reference==
1.37 A crystal structure of pathogenic factor pectate lyase from Acidovorax citrulli.,Tang Q, Liu YP, Ren ZG, Yan XX, Zhang LQ Proteins. 2013 Aug;81(8):1485-90. doi: 10.1002/prot.24298. Epub 2013 Jun 5. PMID:23568384<ref>PMID:23568384</ref>
<ref group="xtra">PMID:023568384</ref><references group="xtra"/><references/>
 
[[Category: Acidovorax citrulli aac00-1]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Liqun, Z.]]
</div>
[[Category: Qun, T.]]
<div class="pdbe-citations 4hwv" style="background-color:#fffaf0;"></div>
[[Category: Lyase]]
== References ==
[[Category: Pl1 family]]
<references/>
[[Category: Right-handed-helix]]
__TOC__
</StructureSection>
[[Category: Acidovorax citrulli AAC00-1]]
[[Category: Large Structures]]
[[Category: Liqun Z]]
[[Category: Qun T]]
Retrieved from "https://proteopedia.org/4hwv"