1gxn

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[[Image:1gxn.gif|left|200px]]
[[Image:1gxn.gif|left|200px]]
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{{Structure
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|PDB= 1gxn |SIZE=350|CAPTION= <scene name='initialview01'>1gxn</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1gxn", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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{{STRUCTURE_1gxn| PDB=1gxn | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxn OCA], [http://www.ebi.ac.uk/pdbsum/1gxn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gxn RCSB]</span>
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'''FAMILY 10 POLYSACCHARIDE LYASE FROM CELLVIBRIO CELLULOSA'''
'''FAMILY 10 POLYSACCHARIDE LYASE FROM CELLVIBRIO CELLULOSA'''
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[[Category: Davies, G J.]]
[[Category: Davies, G J.]]
[[Category: Turkenburg, J P.]]
[[Category: Turkenburg, J P.]]
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[[Category: elimination]]
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[[Category: Elimination]]
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[[Category: lyase]]
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[[Category: Lyase]]
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[[Category: mechanism]]
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[[Category: Mechanism]]
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[[Category: pectate]]
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[[Category: Pectate]]
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Revision as of 15:08, 2 May 2008

Template:STRUCTURE 1gxn

FAMILY 10 POLYSACCHARIDE LYASE FROM CELLVIBRIO CELLULOSA


Overview

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.

About this Structure

1GXN is a Single protein structure of sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 18:08:58 2008

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