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2buq

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[[Image:2buq.gif|left|200px]]<br /><applet load="2buq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2buq, resolution 1.8&Aring;" />
 
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'''CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 IN COMPLEX WITH CATECHOL'''<br />
 
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==Overview==
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==Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 in Complex with Catechol==
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The catechol dioxygenases allow a wide variety of bacteria to use aromatic, compounds as carbon sources by catalyzing the key ring-opening step. These, enzymes use specifically either catechol or protocatechuate, (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as, the sole cofactor. To learn how this family of metalloenzymes functions, a, structural analysis of designed and selected mutants of these enzymes has, been undertaken. Here we review the results of this analysis on the, nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.
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<StructureSection load='2buq' size='340' side='right'caption='[[2buq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2buq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi_ADP1 Acinetobacter baylyi ADP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUQ 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]] 1.8&#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=CAQ:CATECHOL'>CAQ</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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=2buq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2buq OCA], [https://pdbe.org/2buq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2buq RCSB], [https://www.ebi.ac.uk/pdbsum/2buq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2buq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PCXA_ACIAD PCXA_ACIAD] Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
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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/bu/2buq_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=2buq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.
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==About this Structure==
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Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.,Brown CK, Vetting MW, Earhart CA, Ohlendorf DH Annu Rev Microbiol. 2004;58:555-85. PMID:15487948<ref>PMID:15487948</ref>
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2BUQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus] with FE and CAQ as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3] Known structural/functional Site: <scene name='pdbsite=AC1:Caq Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BUQ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1., Brown CK, Vetting MW, Earhart CA, Ohlendorf DH, Annu Rev Microbiol. 2004;58:555-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15487948 15487948]
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</div>
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[[Category: Acinetobacter calcoaceticus]]
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<div class="pdbe-citations 2buq" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Protocatechuate 3,4-dioxygenase]]
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[[Category: Argenio, D.A.D.]]
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[[Category: Lipscomb, J.D.]]
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[[Category: Ohlendorf, D.H.]]
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[[Category: Ornston, L.N.]]
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[[Category: Valley, M.P.]]
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[[Category: Vetting, M.W.]]
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[[Category: CAQ]]
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[[Category: FE]]
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[[Category: aromatic degradation]]
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[[Category: beta-sandwich]]
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[[Category: dioxygenase]]
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[[Category: mixed alpha/beta structure]]
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[[Category: non-heme iron]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:59:03 2007''
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==See Also==
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Acinetobacter baylyi ADP1]]
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[[Category: Large Structures]]
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[[Category: D'Argenio DA]]
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[[Category: Lipscomb JD]]
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[[Category: Ohlendorf DH]]
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[[Category: Ornston LN]]
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[[Category: Valley MP]]
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[[Category: Vetting MW]]

Current revision

Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 in Complex with Catechol

PDB ID 2buq

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