1mpy

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(New page: 200px<br /><applet load="1mpy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpy, resolution 2.8&Aring;" /> '''STRUCTURE OF CATECHOL...)
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[[Image:1mpy.jpg|left|200px]]<br /><applet load="1mpy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mpy, resolution 2.8&Aring;" />
 
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'''STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2'''<br />
 
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==Overview==
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==STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2==
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BACKGROUND: Catechol dioxygenases catalyze the ring cleavage of catechol, and its derivatives in either an intradiol or extradiol manner. These, enzymes have a key role in the degradation of aromatic molecules in the, environment by soil bacteria. Catechol 2, 3-dioxygenase catalyzes the, incorporation of dioxygen into catechol and the extradiol ring cleavage to, form 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase, (metapyrocatechase, MPC) from Pseudomonas putida mt-2 was the first, extradiol dioxygenase to be obtained in a pure form and has been studied, extensively. The lack of an MPC structure has hampered the understanding, of the general mechanism of extradiol dioxygenases. RESULTS: The, three-dimensional structure of MPC has been determined at 2.8 A resolution, by the multiple isomorphous replacement method. The enzyme is a, homotetramer with each subunit folded into two similar domains. The, structure of the MPC subunit resembles that of 2,3-dihydroxybiphenyl, 1,2-dioxygenase, although there is low amino acid sequence identity, between these enzymes. The active-site structure reveals a distorted, tetrahedral Fe(II) site with three endogenous ligands (His153, His214 and, Glu265), and an additional molecule that is most probably acetone., CONCLUSIONS: The present structure of MPC, combined with those of two, 2,3-dihydroxybiphenyl 1,2-dioxygenases, reveals a conserved core region of, the active site comprising three Fe(II) ligands (His153, His214 and, Glu265), one tyrosine (Tyr255) and two histidine (His199 and His246), residues. The results suggest that extradiol dioxygenases employ a common, mechanism to recognize the catechol ring moiety of various substrates and, to activate dioxygen. One of the conserved histidine residues (His199), seems to have important roles in the catalytic cycle.
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<StructureSection load='1mpy' size='340' side='right'caption='[[1mpy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mpy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MPY 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]] 2.8&#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=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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=1mpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpy OCA], [https://pdbe.org/1mpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mpy RCSB], [https://www.ebi.ac.uk/pdbsum/1mpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mpy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYLE1_PSEPU XYLE1_PSEPU]
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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/mp/1mpy_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=1mpy 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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1MPY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with FE2 and ACN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Catechol_2,3-dioxygenase Catechol 2,3-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.2 1.13.11.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MPY OCA].
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2., Kita A, Kita S, Fujisawa I, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K, Structure. 1999 Jan 15;7(1):25-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368270 10368270]
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[[Category: Large Structures]]
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[[Category: Catechol 2,3-dioxygenase]]
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Fujisawa I]]
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[[Category: Fujisawa, I.]]
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[[Category: Horiike K]]
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[[Category: Horiike, K.]]
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[[Category: Inaka K]]
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[[Category: Inaka, K.]]
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[[Category: Ishida T]]
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[[Category: Ishida, T.]]
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[[Category: Kita A]]
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[[Category: Kita, A.]]
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[[Category: Kita S]]
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[[Category: Kita, S.]]
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[[Category: Miki K]]
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[[Category: Miki, K.]]
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[[Category: Nozaki M]]
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[[Category: Nozaki, M.]]
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[[Category: ACN]]
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[[Category: FE2]]
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[[Category: 3-dioxygenase]]
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[[Category: catechol 2]]
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[[Category: extradiol dioxygenase]]
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[[Category: metapyrocatechase]]
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[[Category: non heme iron dioxygenase]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:37:32 2007''
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Current revision

STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2

PDB ID 1mpy

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