1idj

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==About this Structure==
==About this Structure==
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1IDJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]]. Active as [[http://en.wikipedia.org/wiki/Lyase Lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.10 4.2.2.10]]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDJ OCA]].
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1IDJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]]. Active as [[http://en.wikipedia.org/wiki/Pectin_lyase Pectin lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.10 4.2.2.10]]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDJ OCA]].
==Reference==
==Reference==
Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases., Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J, Structure. 1997 May 15;5(5):677-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9195887 9195887]
Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases., Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J, Structure. 1997 May 15;5(5):677-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9195887 9195887]
[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
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[[Category: Pectin lyase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Benen, J.]]
[[Category: Benen, J.]]
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[[Category: signal]]
[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:29:08 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:25:07 2007''

Revision as of 08:20, 30 October 2007


1idj, resolution 2.4Å

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PECTIN LYASE A

Overview

BACKGROUND: Microbial pectin and pectate lyases are virulence factors that, degrade the pectic components of the plant cell wall. The homogalacturan, backbone of pectin varies in its degree of methylation from the highly, methylated and relatively hydrophobic form known as pectin, to the fully, demethylated and highly charged form known as pectate. Methylated and, demethylated regions of pectin are cleaved by pectin lyase and, calcium-dependent pectate lyases, respectively. Protein engineering of, lyases specific for particular patterns of methylation, will yield, modified pectins of high value to the food and pharmaceutical industries., RESULTS: The crystal structures of pectin lyase A from two strains of, Aspergillus niger, N400 and 4M-147, have been determined at pH 6.5 (2.4 A, ... [(full description)]

About this Structure

1IDJ is a [Single protein] structure of sequence from [Aspergillus niger]. Active as [Pectin lyase], with EC number [4.2.2.10]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [OCA].

Reference

Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases., Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J, Structure. 1997 May 15;5(5):677-89. PMID:9195887

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