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1pe9

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[[Image:1pe9.jpg|left|200px]]
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{{STRUCTURE_1pe9| PDB=1pe9 | SCENE= }}
{{STRUCTURE_1pe9| PDB=1pe9 | SCENE= }}
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'''MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A'''
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===MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A===
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==Overview==
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Pectate lyase A (PelA) is a pectate-degrading enzyme secreted by plant pathogens. PelA from Erwinia chrysanthemi has 61% amino-acid identity and a conserved structural similarity to pectate lyase E (PelE). Although similar in structure and sequence, the enzymatic characteristics of PelA differ from those for PelE. A structural alignment of PelA and PelE reveals differences in the T1.5 loop. The sequence of the T1.5 loop in PelA was mutated to the homologous sequence in PelE. The crystal structure of the PelA T1.5 mutant has been solved to 1.6 and 2.9 A resolution. The enzymatic and structural properties of the T1.5 mutant are discussed.
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(as it appears on PubMed at http://www.pubmed.gov), where 12832805 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12832805}}
==About this Structure==
==About this Structure==
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[[Category: Yoder, M D.]]
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[[Category: Parallel beta helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:59:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:33:05 2008''

Revision as of 00:33, 29 July 2008

Image:1pe9.png

Template:STRUCTURE 1pe9

MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A

Template:ABSTRACT PUBMED 12832805

About this Structure

1PE9 is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.

Reference

Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16., Dehdashti SJ, Doan CN, Chao KL, Yoder MD, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1339-42. Epub 2003, Jun 27. PMID:12832805

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