1mqf

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[[Image:1mqf.gif|left|200px]]<br /><applet load="1mqf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mqf, resolution 2.50&Aring;" />
 
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'''Compound I from Proteus mirabilis catalase'''<br />
 
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==Overview==
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==Compound I from Proteus mirabilis catalase==
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The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction.
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<StructureSection load='1mqf' size='340' side='right'caption='[[1mqf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mqf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2caf 2caf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQF 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OMT:S-DIOXYMETHIONINE'>OMT</scene>, <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=1mqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqf OCA], [https://pdbe.org/1mqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mqf RCSB], [https://www.ebi.ac.uk/pdbsum/1mqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CATA_PROMI CATA_PROMI] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
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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/mq/1mqf_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=1mqf 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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1MQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=O:'>O</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2CAF. Active as [http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQF OCA].
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*[[Catalase 3D structures|Catalase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid., Andreoletti P, Pernoud A, Sainz G, Gouet P, Jouve HM, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2163-8. Epub 2003, Nov 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14646074 14646074]
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[[Category: Large Structures]]
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[[Category: Catalase]]
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[[Category: Proteus mirabilis]]
[[Category: Proteus mirabilis]]
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[[Category: Single protein]]
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[[Category: Andreoletti P]]
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[[Category: Andreoletti, P.]]
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[[Category: Gouet P]]
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[[Category: Gouet, P.]]
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[[Category: Jouve HM]]
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[[Category: Jouve, H M.]]
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[[Category: Pernoud A]]
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[[Category: Pernoud, A.]]
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[[Category: Sainz G]]
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[[Category: Sainz, G.]]
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[[Category: GOL]]
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[[Category: HEM]]
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[[Category: O]]
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[[Category: SO4]]
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[[Category: alpha + beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:59 2008''
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Current revision

Compound I from Proteus mirabilis catalase

PDB ID 1mqf

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