1ukf
From Proteopedia
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| - | [[Image:1ukf.jpg|left|200px]] | + | [[Image:1ukf.jpg|left|200px]] |
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| - | '''Crystal Structure of Pseudomonas Avirulence Protein AvrPphB''' | + | {{Structure |
| + | |PDB= 1ukf |SIZE=350|CAPTION= <scene name='initialview01'>1ukf</scene>, resolution 1.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal Structure of Pseudomonas Avirulence Protein AvrPphB''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UKF is a [ | + | 1UKF is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14694194 14694194] |
[[Category: Pseudomonas syringae pv. phaseolicola]] | [[Category: Pseudomonas syringae pv. phaseolicola]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hypersensitive response]] | [[Category: hypersensitive response]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:06 2008'' |
Revision as of 12:33, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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