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==Structure of the tandemly repeated protein tyrosine phosphatase like phytase from Mitsuokella multacida== | |||
<StructureSection load='3f41' size='340' side='right'caption='[[3f41]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3f41]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mitsuokella_multacida Mitsuokella multacida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F41 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3f41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f41 OCA], [https://pdbe.org/3f41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f41 RCSB], [https://www.ebi.ac.uk/pdbsum/3f41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f41 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A3QMF6_9FIRM A3QMF6_9FIRM] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/3f41_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3f41 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mitsuokella multacida expresses a unique inositol polyphosphatase (PhyAmm) that is composed of tandem repeats (TRs). Each repeat possesses a protein tyrosine phosphatase (PTP) active-site signature sequence and fold. Using a combination of structural, mutational, and kinetic studies, we show that the N-terminal (D1) and C-terminal (D2) active sites of the TR have diverged and possess significantly different specificities for inositol polyphosphate. Structural analysis and molecular docking calculations identify steric and electrostatic differences within the substrate binding pocket of each TR that may be involved in the altered substrate specificity. The implications of our results for the biological function of related PTP-like phytases are discussed. Finally, the structures and activities of PhyAmm and tandemly repeated receptor PTPs are compared and discussed. To our knowledge, this is the first example of an inositol phosphatase with tandem PTP domains possessing substrate specificity for different inositol phosphates. | |||
Structural analysis of a multifunctional, tandemly repeated inositol polyphosphatase.,Gruninger RJ, Selinger LB, Mosimann SC J Mol Biol. 2009 Sep 11;392(1):75-86. Epub 2009 Jun 3. PMID:19500593<ref>PMID:19500593</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3f41" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Phytase 3D structures|Phytase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mitsuokella multacida]] | [[Category: Mitsuokella multacida]] | ||
[[Category: Gruninger | [[Category: Gruninger RJ]] | ||
[[Category: Mosimann | [[Category: Mosimann SC]] | ||
[[Category: Selinger | [[Category: Selinger LB]] | ||
Latest revision as of 03:28, 28 December 2023
Structure of the tandemly repeated protein tyrosine phosphatase like phytase from Mitsuokella multacidaStructure of the tandemly repeated protein tyrosine phosphatase like phytase from Mitsuokella multacida
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMitsuokella multacida expresses a unique inositol polyphosphatase (PhyAmm) that is composed of tandem repeats (TRs). Each repeat possesses a protein tyrosine phosphatase (PTP) active-site signature sequence and fold. Using a combination of structural, mutational, and kinetic studies, we show that the N-terminal (D1) and C-terminal (D2) active sites of the TR have diverged and possess significantly different specificities for inositol polyphosphate. Structural analysis and molecular docking calculations identify steric and electrostatic differences within the substrate binding pocket of each TR that may be involved in the altered substrate specificity. The implications of our results for the biological function of related PTP-like phytases are discussed. Finally, the structures and activities of PhyAmm and tandemly repeated receptor PTPs are compared and discussed. To our knowledge, this is the first example of an inositol phosphatase with tandem PTP domains possessing substrate specificity for different inositol phosphates. Structural analysis of a multifunctional, tandemly repeated inositol polyphosphatase.,Gruninger RJ, Selinger LB, Mosimann SC J Mol Biol. 2009 Sep 11;392(1):75-86. Epub 2009 Jun 3. PMID:19500593[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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