1gxn: Difference between revisions
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[[Image:1gxn.gif|left|200px]] | [[Image:1gxn.gif|left|200px]] | ||
'''FAMILY 10 POLYSACCHARIDE LYASE FROM CELLVIBRIO CELLULOSA''' | {{Structure | ||
|PDB= 1gxn |SIZE=350|CAPTION= <scene name='initialview01'>1gxn</scene>, resolution 1.50Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''FAMILY 10 POLYSACCHARIDE LYASE FROM CELLVIBRIO CELLULOSA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GXN is a [ | 1GXN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12221284 12221284] | ||
[[Category: Cellvibrio japonicus]] | [[Category: Cellvibrio japonicus]] | ||
[[Category: Pectate lyase]] | [[Category: Pectate lyase]] | ||
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[[Category: pectate]] | [[Category: pectate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:29:21 2008'' | ||
Revision as of 09:29, 20 March 2008
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| 1gxn, resolution 1.50Å | |||||||||||||
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| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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