4d74

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'''Unreleased structure'''
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==1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI==
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<StructureSection load='4d74' size='340' side='right' caption='[[4d74]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4d74 is ON HOLD until Paper Publication
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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>
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Authors: Benini, S., Salomone-Stagni, M., Caputi, L., Cianci, M.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: 1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI
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<div class="pdbe-citations 4d74" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Protein-tyrosine-phosphatase]]
[[Category: Benini, S]]
[[Category: Benini, S]]
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[[Category: Caputi, L]]
[[Category: Cianci, M]]
[[Category: Cianci, M]]
[[Category: Salomone-Stagni, M]]
[[Category: Salomone-Stagni, M]]
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[[Category: Caputi, L]]
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[[Category: Amsi]]
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[[Category: Amylovoran]]
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[[Category: Fire blight]]
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[[Category: Hydrolase]]
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[[Category: Phosphatase]]
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[[Category: Tyrosine phosphatase]]

Revision as of 16:57, 20 January 2016

1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI

4d74, resolution 1.57Å

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