1d2t

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(New page: 200px<br /><applet load="1d2t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d2t, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1d2t.gif|left|200px]]<br /><applet load="1d2t" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d2t, resolution 1.9&Aring;" />
 
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'''CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE==
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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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<StructureSection load='1d2t' size='340' side='right'caption='[[1d2t]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d2t]] is a 1 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=1D2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D2T 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]] 1.9&#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=SO4:SULFATE+ION'>SO4</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=1d2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2t OCA], [https://pdbe.org/1d2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d2t RCSB], [https://www.ebi.ac.uk/pdbsum/1d2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d2t 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/d2/1d2t_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=1d2t 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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==About this Structure==
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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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1D2T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_blattae Escherichia blattae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D2T 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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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10835340 10835340]
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</div>
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[[Category: Acid phosphatase]]
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<div class="pdbe-citations 1d2t" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia blattae]]
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[[Category: Single protein]]
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[[Category: Asano, Y.]]
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[[Category: Gondoh, K.]]
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[[Category: Ishikawa, K.]]
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[[Category: Mihara, Y.]]
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[[Category: Suzuki, E.]]
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[[Category: SO4]]
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[[Category: all alpha]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:20:53 2007''
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==See Also==
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*[[Acid phosphatase 3D structures|Acid phosphatase 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: Shimwellia blattae]]
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[[Category: Asano Y]]
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[[Category: Gondoh K]]
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[[Category: Ishikawa K]]
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[[Category: Mihara Y]]
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[[Category: Suzuki E]]

Current revision

CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE

PDB ID 1d2t

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