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1u25
From Proteopedia
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<StructureSection load='1u25' size='340' side='right'caption='[[1u25]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1u25' size='340' side='right'caption='[[1u25]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1u25]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1u25]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Selenomonas_ruminantium Selenomonas ruminantium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U25 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u25 OCA], [https://pdbe.org/1u25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u25 RCSB], [https://www.ebi.ac.uk/pdbsum/1u25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u25 ProSAT]</span></td></tr> |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q7WUJ1_SELRU Q7WUJ1_SELRU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1u25 ConSurf]. | </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=1u25 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Various inositide phosphatases participate in the regulation of inositol polyphosphate signaling molecules. Plant phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and phosphate. The phytase from Selenomonas ruminantium shares no sequence homology with other microbial phytases. Its crystal structure revealed a phytase fold of the dual-specificity phosphatase type. The active site is located near a conserved cysteine-containing (Cys241) P loop. We also solved two other crystal forms in which an inhibitor, myo-inositol hexasulfate, is cocrystallized with the enzyme. In the "standby" and the "inhibited" crystal forms, the inhibitor is bound, respectively, in a pocket slightly away from Cys241 and at the substrate binding site where the phosphate group to be hydrolyzed is held close to the -SH group of Cys241. Our structural and mutagenesis studies allow us to visualize the way in which the P loop-containing phytase attracts and hydrolyzes the substrate (phytate) sequentially. | ||
| - | + | ==See Also== | |
| - | + | *[[Phytase 3D structures|Phytase 3D structures]] | |
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| - | == | + | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Ancyromonas ruminantium certes 1889]] | ||
| - | [[Category: 5-phytase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cheng | + | [[Category: Selenomonas ruminantium]] |
| - | [[Category: Chou | + | [[Category: Cheng KJ]] |
| - | [[Category: Chu | + | [[Category: Chou CC]] |
| - | [[Category: Guo | + | [[Category: Chu HM]] |
| - | [[Category: Lai | + | [[Category: Guo RT]] |
| - | [[Category: Lin | + | [[Category: Lai HL]] |
| - | [[Category: Selinger | + | [[Category: Lin TW]] |
| - | [[Category: Shr | + | [[Category: Selinger BL]] |
| - | [[Category: Tang | + | [[Category: Shr HL]] |
| - | [[Category: Wang | + | [[Category: Tang TY]] |
| - | + | [[Category: Wang AH-J]] | |
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Current revision
Crystal structure of Selenomonas ruminantium phytase complexed with persulfated phytate in the C2221 crystal form
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Categories: Large Structures | Selenomonas ruminantium | Cheng KJ | Chou CC | Chu HM | Guo RT | Lai HL | Lin TW | Selinger BL | Shr HL | Tang TY | Wang AH-J
