1ukf
From Proteopedia
(New page: 200px<br /><applet load="1ukf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ukf, resolution 1.35Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ukf.jpg|left|200px]]<br /><applet load="1ukf" size=" | + | [[Image:1ukf.jpg|left|200px]]<br /><applet load="1ukf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ukf, resolution 1.35Å" /> | caption="1ukf, resolution 1.35Å" /> | ||
'''Crystal Structure of Pseudomonas Avirulence Protein AvrPphB'''<br /> | '''Crystal Structure of Pseudomonas Avirulence Protein AvrPphB'''<br /> | ||
==Overview== | ==Overview== | ||
| - | AvrPphB is an avirulence (Avr) protein from the plant pathogen Pseudomonas | + | AvrPphB is an avirulence (Avr) protein from the plant pathogen Pseudomonas syringae that can trigger a disease-resistance response in a number of host plants including Arabidopsis. AvrPphB belongs to a novel family of cysteine proteases with the charter member of this family being the Yersinia effector protein YopT. AvrPphB has a very stringent substrate specificity, catalyzing a single proteolytic cleavage in the Arabidopsis serine/threonine kinase PBS1. We have determined the crystal structure of AvrPphB by x-ray crystallography at 1.35-A resolution. The structure is composed of a central antiparallel beta-sheet, with alpha-helices packing on both sides of the sheet to form a two-lobe structure. The core of this structure resembles the papain-like cysteine proteases. The similarity includes the AvrPphB active site catalytic triad of Cys-98, His-212, and Asp-227 and the oxyanion hole residue Asn-93. Based on analogy with inhibitor complexes of the papain-like proteases, we propose a model for the substrate-binding mechanism of AvrPphB. A deep and positively charged pocket (S2) and a neighboring shallow surface (S3) likely bind to aspartic acid and glycine residues in the substrate located two (P2) and three (P3) residues N terminal to the cleavage site, respectively. Further implications about the specificity of plant pathogen recognition are also discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1UKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._phaseolicola Pseudomonas syringae pv. phaseolicola]. Full crystallographic information is available from [http:// | + | 1UKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._phaseolicola Pseudomonas syringae pv. phaseolicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UKF OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Pseudomonas syringae pv. phaseolicola]] | [[Category: Pseudomonas syringae pv. phaseolicola]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dixon, J | + | [[Category: Dixon, J E.]] |
| - | [[Category: Innes, R | + | [[Category: Innes, R W.]] |
[[Category: Shao, F.]] | [[Category: Shao, F.]] | ||
[[Category: Xu, Z.]] | [[Category: Xu, Z.]] | ||
| Line 23: | Line 23: | ||
[[Category: hypersensitive response]] | [[Category: hypersensitive response]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:34 2008'' |
Revision as of 13:25, 21 February 2008
|
Crystal Structure of Pseudomonas Avirulence Protein AvrPphB
Overview
AvrPphB is an avirulence (Avr) protein from the plant pathogen Pseudomonas syringae that can trigger a disease-resistance response in a number of host plants including Arabidopsis. AvrPphB belongs to a novel family of cysteine proteases with the charter member of this family being the Yersinia effector protein YopT. AvrPphB has a very stringent substrate specificity, catalyzing a single proteolytic cleavage in the Arabidopsis serine/threonine kinase PBS1. We have determined the crystal structure of AvrPphB by x-ray crystallography at 1.35-A resolution. The structure is composed of a central antiparallel beta-sheet, with alpha-helices packing on both sides of the sheet to form a two-lobe structure. The core of this structure resembles the papain-like cysteine proteases. The similarity includes the AvrPphB active site catalytic triad of Cys-98, His-212, and Asp-227 and the oxyanion hole residue Asn-93. Based on analogy with inhibitor complexes of the papain-like proteases, we propose a model for the substrate-binding mechanism of AvrPphB. A deep and positively charged pocket (S2) and a neighboring shallow surface (S3) likely bind to aspartic acid and glycine residues in the substrate located two (P2) and three (P3) residues N terminal to the cleavage site, respectively. Further implications about the specificity of plant pathogen recognition are also discussed.
About this Structure
1UKF is a Single protein structure of sequence from Pseudomonas syringae pv. phaseolicola. Full crystallographic information is available from OCA.
Reference
The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site., Zhu M, Shao F, Innes RW, Dixon JE, Xu Z, Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):302-7. Epub 2003 Dec 23. PMID:14694194
Page seeded by OCA on Thu Feb 21 15:25:34 2008
