3HGK

crystal structure of effect protein AvrptoB complexed with kinase Pto

Summary for 3HGK

• Entry DOI: 10.2210/pdb3hgk/pdb
• Related: 3HGL
• Descriptor: Protein kinase, Effector protein hopAB2 (2 entities in total)
• Functional Keywords: five helices, pto p+1 loop, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, hypersensitive response elicitation, ligase, secreted, ubl conjugation, ubl conjugation pathway, virulence, transferase
• Biological source: Solanum pimpinellifolium (currant tomato); More
• Cellular location: Secreted: Q8RSY1
• Total number of polymer chains: 8
• Total formula weight: 187036.16

Authors

Dong, J.,Fan, F.,Gu, L.,Chai, J. (deposition date: 2009-05-14, release date: 2009-06-23, Last modification date: 2024-10-09)

Primary citation

Dong, J.,Xiao, F.,Fan, F.,Gu, L.,Cang, H.,Martin, G.B.,Chai, J.
Crystal Structure of the Complex between Pseudomonas Effector AvrPtoB and the Tomato Pto Kinase Reveals Both a Shared and a Unique Interface Compared with AvrPto-Pto
Plant Cell, 21:1846-1859, 2009

PubMed Abstract: Resistance to bacterial speck disease in tomato (Solanum lycopersicum) is activated upon recognition by the host Pto kinase of either one of two sequence-unrelated effector proteins, AvrPto or AvrPtoB, from Pseudomonas syringae pv tomato (Pst). Pto induces Pst immunity by acting in concert with the Prf protein. The recently reported structure of the AvrPto-Pto complex revealed that interaction of AvrPto with Pto appears to relieve an inhibitory effect of Pto, allowing Pto to activate Prf. Here, we present the crystal structure of the Pto binding domain of AvrPtoB (residues 121 to 205) at a resolution of 1.9A and of the AvrPtoB(121-205)-Pto complex at a resolution of 3.3 A. AvrPtoB(121-205) exhibits a tertiary fold that is completely different from that of AvrPto, and its conformation remains largely unchanged upon binding to Pto. In common with AvrPto-Pto, the AvrPtoB-Pto complex relies on two interfaces. One of these interfaces is similar in both complexes, although the primary amino acid sequences from the two effector proteins are very different. Amino acid substitutions in Pto at the other interface disrupt the interaction of AvrPtoB-Pto but not that of AvrPto-Pto. Interestingly, substitutions in Pto affecting this unique interface also cause Pto to induce Prf-dependent host cell death independently of either effector protein.

PubMed: 19509331
DOI: 10.1105/tpc.109.066878

Experimental method

X-RAY DIFFRACTION (3.3 Å)