4d74: Difference between revisions

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==1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI==
==1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI==
<StructureSection load='4d74' size='340' side='right' caption='[[4d74]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
<StructureSection load='4d74' size='340' side='right'caption='[[4d74]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d74]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D74 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d74]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Erwinia_amylovora_ATCC_49946 Erwinia amylovora ATCC 49946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D74 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d74 OCA], [http://pdbe.org/4d74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d74 RCSB], [http://www.ebi.ac.uk/pdbsum/4d74 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4d74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d74 OCA], [https://pdbe.org/4d74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d74 RCSB], [https://www.ebi.ac.uk/pdbsum/4d74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d74 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AMSI_ERWAM AMSI_ERWAM]] May function as a phosphatase required for amylovoran (an exopolysaccharide that functions as a virulence factor) production.  
[https://www.uniprot.org/uniprot/AMSI_ERWAM AMSI_ERWAM] May function as a phosphatase required for amylovoran (an exopolysaccharide that functions as a virulence factor) production.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
The Gram-negative bacterium Erwinia amylovora is a destructive pathogen of plants belonging to the Rosaceae family. Amongst its pathogenicity factors, E. amylovora produces the exopolysaccharide amylovoran, which contributes to the occlusion of plant vessels, causing wilting of shoots and eventually resulting in plant death. Amylovoran biosynthesis requires the presence of 12 genes (from amsA to amsL) clustered in the ams region of the E. amylovora genome. They mostly encode glycosyl transferases (AmsG, AmsB, AmsD, AmsE, AmsJ and AmsK), proteins involved in amylovoran translocation and assembly (AmsH, AmsL and AmsC), and also a tyrosine kinase (AmsA) and a tyrosine phosphatase (AmsI), which are both involved in the regulation of amylovoran biosynthesis. The low-molecular-weight protein tyrosine phosphatase AmsI was overexpressed as a His6-tagged protein in Escherichia coli, purified and crystallized. X-ray diffraction data were collected to a maximum resolution of 1.57 A in space group P3121.
AmsI is a low-molecular-weight protein tyrosine phosphatase that regulates the production of amylovoran in the Gram-negative bacterium Erwinia amylovora, a specific pathogen of rosaceous plants such as apple, pear and quince. Amylovoran is an exopolysaccharide that is necessary for successful infection. In order to shed light on AmsI, its structure was solved at 1.57 A resolution at the same pH as its highest measured activity (pH 5.5). In the active site, a water molecule, bridging between the catalytic Arg15 and the reaction-product analogue sulfate, might be representative of the water molecule attacking the phospho-cysteine intermediate in the second step of the reaction mechanism.


Cloning, purification, crystallization and 1.57 A resolution X-ray data analysis of AmsI, the tyrosine phosphatase controlling amylovoran biosynthesis in the plant pathogen Erwinia amylovora.,Benini S, Caputi L, Cianci M Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1693-6. doi:, 10.1107/S2053230X14024947. Epub 2014 Nov 28. PMID:25484228<ref>PMID:25484228</ref>
Characterization and 1.57 A resolution structure of the key fire blight phosphatase AmsI from Erwinia amylovora.,Salomone-Stagni M, Musiani F, Benini S Acta Crystallogr F Struct Biol Commun. 2016 Dec 1;72(Pt 12):903-910. Epub 2016, Nov 30. PMID:27917839<ref>PMID:27917839</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Erwinia amylovora ATCC 49946]]
[[Category: Benini, S]]
[[Category: Large Structures]]
[[Category: Caputi, L]]
[[Category: Benini S]]
[[Category: Cianci, M]]
[[Category: Caputi L]]
[[Category: Salomone-Stagni, M]]
[[Category: Cianci M]]
[[Category: Amsi]]
[[Category: Salomone-Stagni M]]
[[Category: Amylovoran]]
[[Category: Fire blight]]
[[Category: Hydrolase]]
[[Category: Phosphatase]]
[[Category: Tyrosine phosphatase]]

Latest revision as of 15:21, 20 December 2023

1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI

Structural highlights

4d74 is a 1 chain structure with sequence from Erwinia amylovora ATCC 49946. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.57Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMSI_ERWAM May function as a phosphatase required for amylovoran (an exopolysaccharide that functions as a virulence factor) production.

Publication Abstract from PubMed

AmsI is a low-molecular-weight protein tyrosine phosphatase that regulates the production of amylovoran in the Gram-negative bacterium Erwinia amylovora, a specific pathogen of rosaceous plants such as apple, pear and quince. Amylovoran is an exopolysaccharide that is necessary for successful infection. In order to shed light on AmsI, its structure was solved at 1.57 A resolution at the same pH as its highest measured activity (pH 5.5). In the active site, a water molecule, bridging between the catalytic Arg15 and the reaction-product analogue sulfate, might be representative of the water molecule attacking the phospho-cysteine intermediate in the second step of the reaction mechanism.

Characterization and 1.57 A resolution structure of the key fire blight phosphatase AmsI from Erwinia amylovora.,Salomone-Stagni M, Musiani F, Benini S Acta Crystallogr F Struct Biol Commun. 2016 Dec 1;72(Pt 12):903-910. Epub 2016, Nov 30. PMID:27917839[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Salomone-Stagni M, Musiani F, Benini S. Characterization and 1.57 A resolution structure of the key fire blight phosphatase AmsI from Erwinia amylovora. Acta Crystallogr F Struct Biol Commun. 2016 Dec 1;72(Pt 12):903-910. Epub 2016, Nov 30. PMID:27917839 doi:http://dx.doi.org/10.1107/S2053230X16018781

4d74, resolution 1.57Å

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