1eoi

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[[Image:1eoi.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE COMPLEXED WITH THE TRANSITION STATE ANALOG MOLYBDATE==
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The line below this paragraph, containing "STRUCTURE_1eoi", creates the "Structure Box" on the page.
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<StructureSection load='1eoi' size='340' side='right'caption='[[1eoi]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1eoi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Shimwellia_blattae Shimwellia blattae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#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=MOO:MOLYBDATE+ION'>MOO</scene></td></tr>
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{{STRUCTURE_1eoi| PDB=1eoi | SCENE= }}
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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=1eoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eoi OCA], [https://pdbe.org/1eoi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eoi RCSB], [https://www.ebi.ac.uk/pdbsum/1eoi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eoi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9S1A6_SHIBL Q9S1A6_SHIBL]
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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/eo/1eoi_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=1eoi 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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The structure of Escherichia blattae non-specific acid phosphatase (EB-NSAP) has been determined at 1.9 A resolution with a bound sulfate marking the phosphate-binding site. The enzyme is a 150 kDa homohexamer. EB-NSAP shares a conserved sequence motif not only with several lipid phosphatases and the mammalian glucose-6-phosphatases, but also with the vanadium-containing chloroperoxidase (CPO) of Curvularia inaequalis. Comparison of the crystal structures of EB-NSAP and CPO reveals striking similarity in the active site structures. In addition, the topology of the EB-NSAP core shows considerable similarity to the fold of the active site containing part of the monomeric 67 kDa CPO, despite the lack of further sequence identity. These two enzymes are apparently related by divergent evolution. We have also determined the crystal structure of EB-NSAP complexed with the transition-state analog molybdate. Structural comparison of the native enzyme and the enzyme-molybdate complex reveals that the side-chain of His150, a putative catalytic residue, moves toward the molybdate so that it forms a hydrogen bond with the metal oxyanion when the molybdenum forms a covalent bond with NE2 of His189.
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'''CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE COMPLEXED WITH THE TRANSITION STATE ANALOG MOLYBDATE'''
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X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.,Ishikawa K, Mihara Y, Gondoh K, Suzuki E, Asano Y EMBO J. 2000 Jun 1;19(11):2412-23. PMID:10835340<ref>PMID:10835340</ref>
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==Overview==
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The structure of Escherichia blattae non-specific acid phosphatase (EB-NSAP) has been determined at 1.9 A resolution with a bound sulfate marking the phosphate-binding site. The enzyme is a 150 kDa homohexamer. EB-NSAP shares a conserved sequence motif not only with several lipid phosphatases and the mammalian glucose-6-phosphatases, but also with the vanadium-containing chloroperoxidase (CPO) of Curvularia inaequalis. Comparison of the crystal structures of EB-NSAP and CPO reveals striking similarity in the active site structures. In addition, the topology of the EB-NSAP core shows considerable similarity to the fold of the active site containing part of the monomeric 67 kDa CPO, despite the lack of further sequence identity. These two enzymes are apparently related by divergent evolution. We have also determined the crystal structure of EB-NSAP complexed with the transition-state analog molybdate. Structural comparison of the native enzyme and the enzyme-molybdate complex reveals that the side-chain of His150, a putative catalytic residue, moves toward the molybdate so that it forms a hydrogen bond with the metal oxyanion when the molybdenum forms a covalent bond with NE2 of His189.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1EOI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_blattae Escherichia blattae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOI OCA].
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</div>
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<div class="pdbe-citations 1eoi" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate., Ishikawa K, Mihara Y, Gondoh K, Suzuki E, Asano Y, EMBO J. 2000 Jun 1;19(11):2412-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10835340 10835340]
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
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[[Category: Acid phosphatase]]
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== References ==
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[[Category: Escherichia blattae]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Asano, Y.]]
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</StructureSection>
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[[Category: Gondoh, K.]]
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[[Category: Large Structures]]
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[[Category: Ishikawa, K.]]
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[[Category: Shimwellia blattae]]
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[[Category: Mihara, Y.]]
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[[Category: Asano Y]]
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[[Category: Suzuki, E.]]
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[[Category: Gondoh K]]
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[[Category: All-alpha]]
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[[Category: Ishikawa K]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:20:56 2008''
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[[Category: Mihara Y]]
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[[Category: Suzuki E]]

Current revision

CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE COMPLEXED WITH THE TRANSITION STATE ANALOG MOLYBDATE

PDB ID 1eoi

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