1gxo

<StructureSection load='1gxo' size='340' side='right'caption='[[1gxo]], [[Resolution|resolution]] 2.05&Aring;' scene=''>

<table><tr><td colspan='2'>[[1gxo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GXO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxo OCA], [http://pdbe.org/1gxo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gxo RCSB], [http://www.ebi.ac.uk/pdbsum/1gxo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxo ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Enzyme-catalyzed beta-elimination of sugar uronic acids, exemplified by the degradation of plant cell wall pectins, plays an important role in a wide spectrum of biological processes ranging from the recycling of plant biomass through to pathogen virulence. The three-dimensional crystal structure of the catalytic module of a "family PL-10" polysaccharide lyase, Pel10Acm from Cellvibrio japonicus, solved at a resolution of 1.3 A, reveals a new polysaccharide lyase fold and is the first example of a polygalacturonic acid lyase that does not exhibit the "parallel beta-helix" topology. The "Michaelis" complex of an inactive mutant in association with the substrate trigalacturonate/Ca2+ reveals the catalytic machinery harnessed by this polygalacturonate lyase, which displays a stunning resemblance, presumably through convergent evolution, to the tetragalacturonic acid complex observed for a structurally unrelated polygalacturonate lyase from family PL-1. Common coordination of the -1 and +1 subsite saccharide carboxylate groups by a protein-liganded Ca2+ ion, the positioning of an arginine catalytic base in close proximity to the alpha-carbon hydrogen and numerous other conserved enzyme-substrate interactions, considered in light of mutagenesis data for both families, suggest a generic polysaccharide anti-beta-elimination mechanism.

Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases.,Charnock SJ, Brown IE, Turkenburg JP, Black GW, Davies GJ Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12067-72. Epub 2002 Sep 9. PMID:12221284<ref>PMID:12221284</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 1gxo" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cellvibrio cellulosa nagy et al. 2002]]

[[Category: Black, G W]]

[[Category: Brown, I E]]

[[Category: Charnock, S J]]

[[Category: Davies, G J]]

[[Category: Turkenburg, J P]]

[[Category: Pectate]]