2gi4: Difference between revisions

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[[Image:2gi4.gif|left|200px]]<br /><applet load="2gi4" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2gi4.gif|left|200px]]
caption="2gi4" />
 
'''Solution Structure of the Low Molecular Weight Protein Tyrosine Phosphatase from Campylobacter jejuni.'''<br />
{{Structure
|PDB= 2gi4 |SIZE=350|CAPTION= <scene name='initialview01'>2gi4</scene>
|SITE=  
|LIGAND=  
|ACTIVITY= [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]
|GENE= CJ1258 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 Campylobacter jejuni])
}}
 
'''Solution Structure of the Low Molecular Weight Protein Tyrosine Phosphatase from Campylobacter jejuni.'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2GI4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GI4 OCA].  
2GI4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GI4 OCA].  


==Reference==
==Reference==
Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni., Tolkatchev D, Shaykhutdinov R, Xu P, Plamondon J, Watson DC, Young NM, Ni F, Protein Sci. 2006 Oct;15(10):2381-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17008719 17008719]
Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni., Tolkatchev D, Shaykhutdinov R, Xu P, Plamondon J, Watson DC, Young NM, Ni F, Protein Sci. 2006 Oct;15(10):2381-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17008719 17008719]
[[Category: Campylobacter jejuni]]
[[Category: Campylobacter jejuni]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]
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[[Category: protein tyrosine phosphatase]]
[[Category: protein tyrosine phosphatase]]


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Revision as of 18:04, 20 March 2008

File:2gi4.gif


PDB ID 2gi4

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Gene: CJ1258 (Campylobacter jejuni)
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Coordinates: save as pdb, mmCIF, xml



Solution Structure of the Low Molecular Weight Protein Tyrosine Phosphatase from Campylobacter jejuni.


OverviewOverview

A putative low molecular weight protein tyrosine phosphatase (LMW-PTP) was identified in the genome sequence of the bacterial pathogen, Campylobacter jejuni. This novel gene, cj1258, has sequence homology with a distinctive class of phosphatases widely distributed among prokaryotes and eukaryotes. We report here the solution structure of Cj1258 established by high-resolution NMR spectroscopy using NOE-derived distance restraints, hydrogen bond data, and torsion angle restraints. The three-dimensional structure consists of a central four-stranded parallel beta-sheet flanked by five alpha-helices, revealing an overall structural topology similar to those of the eukaryotic LMW-PTPs, such as human HCPTP-A, bovine BPTP, and Saccharomyces cerevisiae LTP1, and to those of the bacterial LMW-PTPs MPtpA from Mycobacterium tuberculosis and YwlE from Bacillus subtilis. The active site of the enzyme is flexible in solution and readily adapts to the binding of ligands, such as the phosphate ion. An NMR-based screen was carried out against a number of potential inhibitors and activators, including phosphonomethylphenylalanine, derivatives of the cinnamic acid, 2-hydroxy-5-nitrobenzaldehyde, cinnamaldehyde, adenine, and hypoxanthine. Despite its bacterial origin, both the three-dimensional structure and ligand-binding properties of Cj1258 suggest that this novel phosphatase may have functional roles close to those of eukaryotic and mammalian tyrosine phosphatases. The three-dimensional structure along with mapping of small-molecule binding will be discussed in the context of developing high-affinity inhibitors of this novel LMW-PTP.

About this StructureAbout this Structure

2GI4 is a Single protein structure of sequence from Campylobacter jejuni. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni., Tolkatchev D, Shaykhutdinov R, Xu P, Plamondon J, Watson DC, Young NM, Ni F, Protein Sci. 2006 Oct;15(10):2381-94. PMID:17008719

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