1pe9: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= PELA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi]) | |GENE= PELA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1jrg|1JRG]], [[1jta|1JTA]], [[1ooc|1OOC]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pe9 OCA], [http://www.ebi.ac.uk/pdbsum/1pe9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pe9 RCSB]</span> | |||
}} | }} | ||
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[[Category: parallel beta helix]] | [[Category: parallel beta helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:31 2008'' | ||
Revision as of 22:58, 30 March 2008
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| , resolution 1.60Å | |||||||
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| Gene: | PELA (Erwinia chrysanthemi) | ||||||
| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||
| Related: | 1JRG, 1JTA, 1OOC
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A
OverviewOverview
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 StructureAbout this Structure
1PE9 is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.
ReferenceReference
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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