1shn

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[[Image:1shn.gif|left|200px]]<br /><applet load="1shn" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1shn, resolution 2.15&Aring;" />
 
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'''Crystal structure of shrimp alkaline phosphatase with phosphate bound'''<br />
 
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==Overview==
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==Crystal structure of shrimp alkaline phosphatase with phosphate bound==
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Alkaline phosphatases (APs) are homodimeric metalloenzymes that catalyze the hydrolysis and transphosphorylation of phosphate monoesters. Each monomer contains a metal-binding triad that for optimal activity is usually occupied by two zinc ions and one magnesium ion. The recently determined crystal structure of cold-active shrimp alkaline phosphatase (SAP) was, however, fully occupied by zinc ions. This paper describes a metal-exchange experiment in which the zinc ion in one binding site (referred to as the M3 site) is replaced by magnesium. Crystal structures revealed a concomitant structural change: the metal exchange causes movement of a ligating histidine into a conformation in which it does not coordinate to the metal ion. The M3 site is relevant to catalysis: its occupation by magnesium is postulated to favour catalysis and it has been suggested to be a regulatory site for other APs. Further crystallographic studies show that ligand binding can induce a conformational change of an active-site arginine from a 'non-docked' (non-interacting) to a 'docked' conformation (interacting with the ligand). The first conformation has only been observed in SAP, while the latter is common in available AP structures. The observation that the arginine does not always bind the substrate may explain the increased catalytic efficiency that is generally observed for cold-active enzymes.
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<StructureSection load='1shn' size='340' side='right'caption='[[1shn]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1shn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pandalus_borealis Pandalus borealis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SHN 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]] 2.15&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1shn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shn OCA], [https://pdbe.org/1shn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1shn RCSB], [https://www.ebi.ac.uk/pdbsum/1shn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1shn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9BHT8_PANBO Q9BHT8_PANBO]
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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/sh/1shn_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=1shn 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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1SHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pandalus_borealis Pandalus borealis] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=SO4:'>SO4</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHN 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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Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase., de Backer MM, McSweeney S, Lindley PF, Hough E, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1555-61. Epub 2004, Aug 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15333925 15333925]
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[[Category: Large Structures]]
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[[Category: Alkaline phosphatase]]
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[[Category: Pandalus borealis]]
[[Category: Pandalus borealis]]
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[[Category: Single protein]]
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[[Category: Hough E]]
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[[Category: Backer, M M.E de.]]
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[[Category: Lindley PF]]
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[[Category: Hough, E.]]
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[[Category: McSweeney S]]
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[[Category: Lindley, P F.]]
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[[Category: De Backer MME]]
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[[Category: McSweeney, S.]]
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[[Category: NAG]]
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[[Category: PO4]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: alkaline phosphatase]]
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[[Category: beta sheet]]
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[[Category: cold-active]]
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[[Category: hydrolase]]
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[[Category: metal triad]]
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[[Category: phosphate]]
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[[Category: phosphomonoester]]
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[[Category: shrimp]]
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[[Category: zinc]]
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[[Category: zinc triad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:34 2008''
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Current revision

Crystal structure of shrimp alkaline phosphatase with phosphate bound

PDB ID 1shn

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