1u25

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(New page: 200px<br /><applet load="1u25" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u25, resolution 2.5&Aring;" /> '''Crystal structure of ...)
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[[Image:1u25.gif|left|200px]]<br /><applet load="1u25" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1u25, resolution 2.5&Aring;" />
 
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'''Crystal structure of Selenomonas ruminantium phytase complexed with persulfated phytate in the C2221 crystal form'''<br />
 
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==Overview==
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==Crystal structure of Selenomonas ruminantium phytase complexed with persulfated phytate in the C2221 crystal form==
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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.
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<StructureSection load='1u25' size='340' side='right'caption='[[1u25]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7WUJ1_SELRU Q7WUJ1_SELRU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u25_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis.,Chu HM, Guo RT, Lin TW, Chou CC, Shr HL, Lai HL, Tang TY, Cheng KJ, Selinger BL, Wang AH Structure. 2004 Nov;12(11):2015-24. PMID:15530366<ref>PMID:15530366</ref>
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1U25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Selenomonas_ruminantium Selenomonas ruminantium] with IHS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/5-phytase 5-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.72 3.1.3.72] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U25 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis., Chu HM, Guo RT, Lin TW, Chou CC, Shr HL, Lai HL, Tang TY, Cheng KJ, Selinger BL, Wang AH, Structure. 2004 Nov;12(11):2015-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15530366 15530366]
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</div>
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[[Category: 5-phytase]]
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<div class="pdbe-citations 1u25" style="background-color:#fffaf0;"></div>
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[[Category: Selenomonas ruminantium]]
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[[Category: Single protein]]
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[[Category: Cheng, K.J.]]
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[[Category: Chou, C.C.]]
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[[Category: Chu, H.M.]]
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[[Category: Guo, R.T.]]
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[[Category: Lai, H.L.]]
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[[Category: Lin, T.W.]]
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[[Category: Selinger, B.L.]]
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[[Category: Shr, H.L.]]
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[[Category: Tang, T.Y.]]
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[[Category: Wang, A.H.J.]]
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[[Category: IHS]]
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[[Category: p-loop]]
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[[Category: phytase]]
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[[Category: ptp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:10:51 2007''
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==See Also==
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*[[Phytase 3D structures|Phytase 3D 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: Large Structures]]
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[[Category: Selenomonas ruminantium]]
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[[Category: Cheng KJ]]
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[[Category: Chou CC]]
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[[Category: Chu HM]]
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[[Category: Guo RT]]
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[[Category: Lai HL]]
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[[Category: Lin TW]]
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[[Category: Selinger BL]]
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[[Category: Shr HL]]
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[[Category: Tang TY]]
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[[Category: Wang AH-J]]

Current revision

Crystal structure of Selenomonas ruminantium phytase complexed with persulfated phytate in the C2221 crystal form

PDB ID 1u25

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