PDBsum entry: 1ooc

Lyase

PDB id: 1ooc

Contents

Protein chains

361 a.a. *

* Residue conservation analysis

PDB id:

1ooc

Name:

Lyase

Title:

Mutations in the t1.5 loop of pectate lyase a

Structure:

Pectate lyase a. Chain: a, b. Fragment: t1.5. Engineered: yes. Mutation: yes

Source:

Erwinia chrysanthemi. Organism_taxid: 556. Gene: pela. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.94Å R-factor: 0.219 R-free: 0.275

Authors:

S.J.Dehdashti,C.N.Doan,K.Chao,P.B.Vordtriede,M.D.Yoder

Key ref:

S.J.Dehdashti et al. (2003). Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16. Acta Crystallogr D Biol Crystallogr, 59, 1339-1342. PubMed id: 12832805 DOI: 10.1107/S0907444903011491

Date:

03-Mar-03 Release date: 16-Mar-04

Protein chains

P0C1A2  (PLYA_ERWCH) -  Pectate lyase A

Seq: 393 a.a.

Struc: 361 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.4.2.2.2 - Pectate lyase.
• Pathway: Pectin and Pectate Lyases
• Reaction: Eliminative cleavage of pectate to give oligosaccharides with 4-deoxy- alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (1 term)
• Biochemical function: lyase activity (3 terms)

DOI no: 10.1107/S0907444903011491

Acta Crystallogr D Biol Crystallogr 59:1339-1342 (2003)

PubMed id: 12832805

Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16.

S.J.Dehdashti, C.N.Doan, K.L.Chao, M.D.Yoder.

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.

Selected figure(s)

Figure 1.
Figure 1 (a) A ribbon diagram of the PelA T1.5 mutant. The parallel -sheets are shown in different colors: yellow for PB1, blue for PB2 and red for PB3. The two -ribbons not participating in the parallel -helix are shown in aqua. The disulfide bond is drawn as an orange thunderbolt and the T1.5 loop is shown in green. (b) A 90° rotation about the vertical axis of the orientation in (a). The N- and C-termini are labeled `N' and `C', respectively. (c) Stereo-image representation of the C^ -chain trace for the PelA T1.5 mutant. Residue numbers throughout the molecule are indicated. Figures were created using MOLSCRIPT version 2.1 (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]) and rendered with Raster3D version 2.6 (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 1339-1342) copyright 2003.

Figure was selected by an automated process.