1jta: Difference between revisions

Revision as of 21:53, 2 May 2008

Crystal Structure of Pectate Lyase A (C2 form)

OverviewOverview

Pectate lyase A is a virulence factor secreted by the plant-pathogenic bacteria Erwinia chrysanthemi. The enzyme cleaves the glycosidic bond of pectate polymers by a calcium-dependent beta-elimination mechanism. The crystal structure of pectate lyase A from E. chrysanthemi EC16 has been determined in two crystal forms, monoclinic C2 to 1.8 A and rhombohedral R3 to 2.1 A. The protein structure is compared with two other pectate lyase isoforms from E. chrysanthemi EC16, pectate lyase C and pectate lyase E. Pectate lyase A is unique as it is the only acidic pectate lyase and has end products that are significantly more varied in length in comparison to those of the other four major pectate lyase isozymes. Differences and similarities in polypeptide trace, size and volume of the active-site groove and surface electrostatics are discussed.

About this StructureAbout this Structure

1JTA is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.

ReferenceReference

Structure of pectate lyase A: comparison to other isoforms., Thomas LM, Doan CN, Oliver RL, Yoder MD, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1008-15. Epub, 2002 May 29. PMID:12037303 Page seeded by OCA on Fri May 2 21:53:27 2008

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OCA

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 '''Crystal Structure of Pectate Lyase A (C2 form)'''
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 [[Category: Thomas, L M.]]
 [[Category: Yoder, M D.]]
-[[Category: parallel beta helix beta-elimination mechanism]]
+[[Category: Parallel beta helix beta-elimination mechanism]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:53:27 2008''
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