4wu3: Difference between revisions
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<StructureSection load='4wu3' size='340' side='right'caption='[[4wu3]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4wu3' size='340' side='right'caption='[[4wu3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wu3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WU3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4wu3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27723 Atcc 27723]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WU3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f41|3f41]], [[4wu2|4wu2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f41|3f41]], [[4wu2|4wu2]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=52226 ATCC 27723])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span></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=4wu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wu3 OCA], [http://pdbe.org/4wu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wu3 ProSAT]</span></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=4wu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wu3 OCA], [http://pdbe.org/4wu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wu3 ProSAT]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: 3-phytase]] | [[Category: 3-phytase]] | ||
[[Category: Atcc 27723]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bruder, L M]] | [[Category: Bruder, L M]] | ||
[[Category: Mosimann, S C]] | [[Category: Mosimann, S C]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] |
Revision as of 10:50, 8 January 2020
Structure of the PTP-like myo-inositol phosphatase from Mitsuokella multacida in complex with myo-inositol-(1,3,4,5)-tetrakisphosphateStructure of the PTP-like myo-inositol phosphatase from Mitsuokella multacida in complex with myo-inositol-(1,3,4,5)-tetrakisphosphate
Structural highlights
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. References
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