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[[Image:1o8f.png|left|200px]]
==PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 9.5 WITH 30MM CA2+==
<StructureSection load='1o8f' size='340' side='right' caption='[[1o8f]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1o8f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O8F FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1air|1air]], [[1o88|1o88]], [[1o8d|1o8d]], [[1o8e|1o8e]], [[1o8g|1o8g]], [[1o8h|1o8h]], [[1o8i|1o8i]], [[1o8j|1o8j]], [[1o8k|1o8k]], [[1o8l|1o8l]], [[1o8m|1o8m]], [[1plu|1plu]], [[2pec|2pec]]</td></tr>
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o8f RCSB], [http://www.ebi.ac.uk/pdbsum/1o8f PDBsum]</span></td></tr>
<table>
== 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/o8/1o8f_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ca(2+) is essential for in vitro activity of Erwinia chrysanthemi pectate lyase C (PelC). Crystallographic analyses of 11 PelC-Ca(2+) complexes, formed at pH 4.5, 9.5, and 11.2 under varying Ca(2+) concentrations, have been solved and refined at a resolution of 2.2 A. The Ca(2+) site represents a new motif for Ca(2+), consisting primarily of beta-turns and beta-strands. The principal differences between PelC and the PelC-Ca(2+) structures at all pH values are the side-chain conformations of Asp-129 and Glu-166 as well as the occupancies of four water molecules. According to calculations of pK(a) values, the presence of Ca(2+) and associated structural changes lower the pK(a) of Arg-218, the amino acid responsible for proton abstraction during catalysis. The Ca(2+) affinity for PelC is weak, as the K(d) was estimated to be 0.132 (+/-0.004) mm at pH 9.5, 1.09 (+/-0.29) mm at pH 11.2, and 5.84 (+/-0.41) mm at pH 4.5 from x-ray diffraction studies and 0.133 (+/-0.045) mm at pH 9.5 from intrinsic tryptophan fluorescence measurements. Given the pH dependence of Ca(2+) affinity, PelC activity at pH 4.5 has been reexamined. At saturating Ca(2+) concentrations, PelC activity increases 10-fold at pH 4.5 but is less than 1% of maximal activity at pH 9.5. Taken together, the studies suggest that the primary Ca(2+) ion in PelC has multiple functions.


{{STRUCTURE_1o8f|  PDB=1o8f  |  SCENE=  }}
Characterization and implications of Ca2+ binding to pectate lyase C.,Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F J Biol Chem. 2003 Apr 4;278(14):12271-7. Epub 2003 Jan 22. PMID:12540845<ref>PMID:12540845</ref>


===PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 9.5 WITH 30MM CA2+===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_12540845}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1o8f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8F OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:012540845</ref><references group="xtra"/>
[[Category: Erwinia chrysanthemi]]
[[Category: Erwinia chrysanthemi]]
[[Category: Pectate lyase]]
[[Category: Pectate lyase]]
Retrieved from "https://proteopedia.org/1o8f"