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1alk

From Proteopedia

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(New page: 200px<br /><applet load="1alk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1alk, resolution 2.0&Aring;" /> '''REACTION MECHANISM OF...)
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[[Image:1alk.jpg|left|200px]]<br /><applet load="1alk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1alk, resolution 2.0&Aring;" />
 
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'''REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS'''<br />
 
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==Overview==
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==REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS==
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Alkaline phosphatase (AP) is a widely distributed non-specific, phosphomonoesterase that functions through formation of a covalent, phosphoseryl intermediate (E-P). The enzyme also catalyzes phosphoryl, transfer reaction to various alcohols. Escherichia coli AP is a homodimer, with 449 residues per monomer. It is a metalloenzyme with two Zn2+ and one, Mg2+ at each active site. The crystal structure of native E. coli AP, complexed with inorganic phosphate (Pi), which is a strong competitive, inhibitor as well as a substrate for the reverse reaction, has been, refined at 2.0 A resolution. Some parts of the molecular have been, retraced, starting from the previous 2.8 A study. The active site has been, modified substantially and is described in this paper. The changes in the, active site region suggest the need to reinterpret earlier spectral data, and suggestions are made. Also presented are the structures of the, Cd-substituted enzyme complexed with inorganic phosphate at 2.5 A, resolution, and the phosphate-free native enzyme at 2.8 A resolution. At, pH 7.5, where the X-ray data were collected, the Cd-substituted enzyme is, predominantly the covalent phosphoenzyme (E-P) while the native Zn/Mg, enzyme exists in predominantly noncovalent (E.P) form. Implication of, these results for the catalytic mechanism of the enzyme is discussed. APs, from other sources are believed to function in a similar manner.
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<StructureSection load='1alk' size='340' side='right'caption='[[1alk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1alk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALK 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&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1alk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alk OCA], [https://pdbe.org/1alk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alk RCSB], [https://www.ebi.ac.uk/pdbsum/1alk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPB_ECOLI PPB_ECOLI]
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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/al/1alk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1alk ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ALK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, MG and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ALK OCA].
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*[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis., Kim EE, Wyckoff HW, J Mol Biol. 1991 Mar 20;218(2):449-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2010919 2010919]
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[[Category: Alkaline phosphatase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kim, E.E.]]
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[[Category: Kim EE]]
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[[Category: Wyckoff, W.]]
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[[Category: Wyckoff W]]
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[[Category: MG]]
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[[Category: PO4]]
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[[Category: ZN]]
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[[Category: alkaline phosphatase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:56:57 2007''
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Current revision

REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS

PDB ID 1alk

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