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== | ==Hafnia Alvei phytase in complex with myo-inositol hexakis sulphate== | ||
[[4aro]] is a 1 chain structure with sequence from [ | <StructureSection load='4aro' size='340' side='right'caption='[[4aro]], [[Resolution|resolution]] 1.59Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4aro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hafnia_alvei Hafnia alvei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARO 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]] 1.59Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IHS:D-MYO-INOSITOL-HEXASULPHATE'>IHS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4aro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aro OCA], [https://pdbe.org/4aro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aro RCSB], [https://www.ebi.ac.uk/pdbsum/4aro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aro ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/H9TUK5_HAFAL H9TUK5_HAFAL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phytases hydrolyse phytate (myo-inositol hexakisphosphate), the principal form of phosphate stored in plant seeds to produce phosphate and lower phosphorylated myo-inositols. They are used extensively in the feed industry, and have been characterised biochemically and structurally with a number of structures in the PDB. They are divided into four distinct families: histidine acid phosphatases (HAP), beta-propeller phytases, cysteine phosphatases and purple acid phosphatases and also split into three enzyme classes, the 3-, 5- and 6-phytases, depending on the position of the first phosphate in the inositol ring to be removed. We report identification, cloning, purification and 3D structures of 6-phytases from two bacteria, Hafnia alvei and Yersinia kristensenii, together with their pH optima, thermal stability, and degradation profiles for phytate. An important result is the structure of the H. alvei enzyme in complex with the substrate analogue myo-inositol hexakissulphate. In contrast to the only previous structure of a ligand-bound 6-phytase, where the 3-phosphate was unexpectedly in the catalytic site, in the H. alvei complex the expected scissile 6-phosphate (sulphate in the inhibitor) is placed in the catalytic site. | |||
Degradation of Phytate by the 6-Phytase from Hafnia alvei: A Combined Structural and Solution Study.,Ariza A, Moroz OV, Blagova EV, Turkenburg JP, Waterman J, Roberts SM, Vind J, Sjoholm C, Lassen SF, De Maria L, Glitsoe V, Skov LK, Wilson KS PLoS One. 2013 May 31;8(5):e65062. doi: 10.1371/journal.pone.0065062. Print 2013. PMID:23741456<ref>PMID:23741456</ref> | |||
<ref | |||
[[ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 4aro" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] | |||
*[[Phytase 3D structures|Phytase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hafnia alvei]] | [[Category: Hafnia alvei]] | ||
[[Category: Ariza | [[Category: Large Structures]] | ||
[[Category: Blagova | [[Category: Ariza A]] | ||
[[Category: | [[Category: Blagova EB]] | ||
[[Category: | [[Category: De Maria L]] | ||
[[Category: | [[Category: Glitsoe V]] | ||
[[Category: Moroz | [[Category: Lassen SF]] | ||
[[Category: Roberts | [[Category: Moroz OV]] | ||
[[Category: Sjoholm | [[Category: Roberts S]] | ||
[[Category: Skov | [[Category: Sjoholm C]] | ||
[[Category: Turkenburg | [[Category: Skov LK]] | ||
[[Category: Vevodova | [[Category: Turkenburg JP]] | ||
[[Category: Vind | [[Category: Vevodova J]] | ||
[[Category: Wilson | [[Category: Vind J]] | ||
[[Category: Wilson KS]] | |||
Latest revision as of 14:33, 20 December 2023
Hafnia Alvei phytase in complex with myo-inositol hexakis sulphateHafnia Alvei phytase in complex with myo-inositol hexakis sulphate
Structural highlights
FunctionPublication Abstract from PubMedPhytases hydrolyse phytate (myo-inositol hexakisphosphate), the principal form of phosphate stored in plant seeds to produce phosphate and lower phosphorylated myo-inositols. They are used extensively in the feed industry, and have been characterised biochemically and structurally with a number of structures in the PDB. They are divided into four distinct families: histidine acid phosphatases (HAP), beta-propeller phytases, cysteine phosphatases and purple acid phosphatases and also split into three enzyme classes, the 3-, 5- and 6-phytases, depending on the position of the first phosphate in the inositol ring to be removed. We report identification, cloning, purification and 3D structures of 6-phytases from two bacteria, Hafnia alvei and Yersinia kristensenii, together with their pH optima, thermal stability, and degradation profiles for phytate. An important result is the structure of the H. alvei enzyme in complex with the substrate analogue myo-inositol hexakissulphate. In contrast to the only previous structure of a ligand-bound 6-phytase, where the 3-phosphate was unexpectedly in the catalytic site, in the H. alvei complex the expected scissile 6-phosphate (sulphate in the inhibitor) is placed in the catalytic site. Degradation of Phytate by the 6-Phytase from Hafnia alvei: A Combined Structural and Solution Study.,Ariza A, Moroz OV, Blagova EV, Turkenburg JP, Waterman J, Roberts SM, Vind J, Sjoholm C, Lassen SF, De Maria L, Glitsoe V, Skov LK, Wilson KS PLoS One. 2013 May 31;8(5):e65062. doi: 10.1371/journal.pone.0065062. Print 2013. PMID:23741456[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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