1ooc: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1ooc|  PDB=1ooc  |  SCENE=  }}  
{{STRUCTURE_1ooc|  PDB=1ooc  |  SCENE=  }}  


'''Mutations in the T1.5 loop of pectate lyase A'''
===Mutations in the T1.5 loop of pectate lyase A===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_12832805}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12832805}}


==About this Structure==
==About this Structure==
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[[Category: Yoder, M D.]]
[[Category: Yoder, M D.]]
[[Category: Parallel beta helix]]
[[Category: Parallel beta helix]]
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