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[[Image:1mqf.gif|left|200px]]


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==Compound I from Proteus mirabilis catalase==
The line below this paragraph, containing "STRUCTURE_1mqf", creates the "Structure Box" on the page.
<StructureSection load='1mqf' size='340' side='right'caption='[[1mqf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1mqf| PDB=1mqf |  SCENE= }}
<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>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mq/1mqf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


'''Compound I from Proteus mirabilis catalase'''
==See Also==
 
*[[Catalase 3D structures|Catalase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1MQF is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/14646074 14646074]
[[Category: Catalase]]
[[Category: Proteus mirabilis]]
[[Category: Proteus mirabilis]]
[[Category: Single protein]]
[[Category: Andreoletti P]]
[[Category: Andreoletti, P.]]
[[Category: Gouet P]]
[[Category: Gouet, P.]]
[[Category: Jouve HM]]
[[Category: Jouve, H M.]]
[[Category: Pernoud A]]
[[Category: Pernoud, A.]]
[[Category: Sainz G]]
[[Category: Sainz, G.]]
[[Category: Alpha + beta]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:35:48 2008''

Latest revision as of 11:39, 10 April 2024

Compound I from Proteus mirabilis catalaseCompound I from Proteus mirabilis catalase

Structural highlights

1mqf is a 1 chain structure with sequence from Proteus mirabilis. This structure supersedes the now removed PDB entry 2caf. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CATA_PROMI Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1mqf, resolution 2.50Å

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