1OOC

Mutations in the T1.5 loop of pectate lyase A

Summary for 1OOC

• Entry DOI: 10.2210/pdb1ooc/pdb
• Related: 1JRG 1JTA
• Descriptor: Pectate lyase A (1 entity in total)
• Functional Keywords: parallel beta helix, lyase
• Biological source: Erwinia chrysanthemi
• Total number of polymer chains: 2
• Total formula weight: 77479.07

Authors

Dehdashti, S.J.,Doan, C.N.,Chao, K.,Vordtriede, P.B.,Yoder, M.D. (deposition date: 2003-03-03, release date: 2004-03-16, Last modification date: 2024-10-16)

Primary citation

Dehdashti, S.J.,Doan, C.N.,Chao, K.L.,Yoder, M.D.
Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16.
Acta Crystallogr.,Sect.D, 59:1339-1342, 2003

PubMed Abstract: 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.

PubMed: 12832805
DOI: 10.1107/S0907444903011491

Experimental method

X-RAY DIFFRACTION (2.94 Å)