PDBsum entry 4z8u

Protein binding

PDB id: 4z8u

Contents

Protein chains

332 a.a.

98 a.a.

Ligands

SO4 ×5

GOL

ACT

Waters ×320

PDB id:

4z8u

Name:

Protein binding

Title:

Crystal structure of avrrxo1-orf1:-orf2 with atp

Structure:

Avrrxo1-orf1. Chain: a. Fragment: unp residues 90-421. Engineered: yes. Avrrxo1-orf2. Chain: b. Fragment: unp residues 1-98. Engineered: yes

Source:

Xanthomonas oryzae pv. Oryzicola. Organism_taxid: 129394. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Resolution:

1.65Å R-factor: 0.202 R-free: 0.236

Authors:

Q.Han,C.Zhou,S.Wu,Y.Liu,Z.Yang,J.Miao,L.Triplett,Q.Cheng,J.Tokuhisa, L.Deblais,H.Robinson,J.E.Leach,J.Li,B.Zhao

Key ref:

Q.Han et al. (2015). Crystal Structure of Xanthomonas AvrRxo1-ORF1, a Type III Effector with a Polynucleotide Kinase Domain, and Its Interactor AvrRxo1-ORF2. Structure, 23, 1900-1909. PubMed id: 26344722 DOI: 10.1016/j.str.2015.06.030

Date:

09-Apr-15 Release date: 23-Sep-15

Protein chain

Q6TKR8  (Q6TKR8_XANOQ) -  AvrRxo1-ORF1 from Xanthomonas oryzae pv. oryzicola

Seq: 421 a.a.

Struc: 332 a.a.

Protein chain

Q6TKR9  (Q6TKR9_XANOQ) -  AvrRxo1-ORF2 from Xanthomonas oryzae pv. oryzicola

Seq: 98 a.a.

Struc: 98 a.a.

DOI no: 10.1016/j.str.2015.06.030

Structure 23:1900-1909 (2015)

PubMed id: 26344722

Crystal Structure of Xanthomonas AvrRxo1-ORF1, a Type III Effector with a Polynucleotide Kinase Domain, and Its Interactor AvrRxo1-ORF2.

Q.Han, C.Zhou, S.Wu, Y.Liu, L.Triplett, J.Miao, J.Tokuhisa, L.Deblais, H.Robinson, J.E.Leach, J.Li, B.Zhao.

ABSTRACT

Xanthomonas oryzae pv. oryzicola (Xoc) causes bacterial leaf streak (BLS) disease on rice plants. Xoc delivers a type III effector AvrRxo1-ORF1 into rice plant cells that can be recognized by disease resistance (R) protein Rxo1, and triggers resistance to BLS disease. However, the mechanism and virulence role of AvrRxo1 is not known. In the genome of Xoc, AvrRxo1-ORF1 is adjacent to another gene AvrRxo1-ORF2, which was predicted to encode a molecular chaperone of AvrRxo1-ORF1. We report the co-purification and crystallization of the AvrRxo1-ORF1:AvrRxo1-ORF2 tetramer complex at 1.64 Å resolution. AvrRxo1-ORF1 has a T4 polynucleotide kinase domain, and expression of AvrRxo1-ORF1 suppresses bacterial growth in a manner dependent on the kinase motif. Although AvrRxo1-ORF2 binds AvrRxo1-ORF1, it is structurally different from typical effector-binding chaperones, in that it has a distinct fold containing a novel kinase-binding domain. AvrRxo1-ORF2 functions to suppress the bacteriostatic activity of AvrRxo1-ORF1 in bacterial cells.