1ooc
From Proteopedia
(New page: 200px<br /><applet load="1ooc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ooc, resolution 2.94Å" /> '''Mutations in the T1....) |
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| - | [[Image:1ooc.jpg|left|200px]]<br /><applet load="1ooc" size=" | + | [[Image:1ooc.jpg|left|200px]]<br /><applet load="1ooc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ooc, resolution 2.94Å" /> | caption="1ooc, resolution 2.94Å" /> | ||
'''Mutations in the T1.5 loop of pectate lyase A'''<br /> | '''Mutations in the T1.5 loop of pectate lyase A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pectate lyase A (PelA) is a pectate-degrading enzyme secreted by plant | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1OOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Active as [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] Full crystallographic information is available from [http:// | + | 1OOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OOC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chao, K.]] | [[Category: Chao, K.]] | ||
| - | [[Category: Dehdashti, S | + | [[Category: Dehdashti, S J.]] |
| - | [[Category: Doan, C | + | [[Category: Doan, C N.]] |
| - | [[Category: Vordtriede, P | + | [[Category: Vordtriede, P B.]] |
| - | [[Category: Yoder, M | + | [[Category: Yoder, M D.]] |
[[Category: parallel beta helix]] | [[Category: parallel beta helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:00 2008'' |
Revision as of 12:20, 21 February 2008
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Mutations in the T1.5 loop of pectate lyase A
Overview
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.
About this Structure
1OOC is a Single protein structure of sequence from Erwinia chrysanthemi. Active as Pectate lyase, with EC number 4.2.2.2 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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