2buv

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[[Image:2buv.gif|left|200px]]
 
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==Crystal Structure Of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S in Complex with Protocatechuate==
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The line below this paragraph, containing "STRUCTURE_2buv", creates the "Structure Box" on the page.
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<StructureSection load='2buv' size='340' side='right'caption='[[2buv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2buv]] 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=2BUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUV FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=DHB:3,4-DIHYDROXYBENZOIC+ACID'>DHB</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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{{STRUCTURE_2buv| PDB=2buv | SCENE= }}
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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=2buv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2buv OCA], [https://pdbe.org/2buv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2buv RCSB], [https://www.ebi.ac.uk/pdbsum/2buv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2buv 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/2buv_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=2buv 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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'''CRYSTAL STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 MUTANT R457S IN COMPLEX WITH PROTOCATECHUATE'''
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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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==Overview==
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2BUV is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUV OCA].
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</div>
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<div class="pdbe-citations 2buv" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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://www.ncbi.nlm.nih.gov/pubmed/15487948 15487948]
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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[[Category: Acinetobacter calcoaceticus]]
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== References ==
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[[Category: Protein complex]]
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<references/>
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[[Category: Protocatechuate 3,4-dioxygenase]]
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__TOC__
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[[Category: Argenio, D A.D.]]
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</StructureSection>
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[[Category: Lipscomb, J D.]]
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[[Category: Acinetobacter baylyi ADP1]]
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[[Category: Ohlendorf, D H.]]
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[[Category: Large Structures]]
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[[Category: Ornston, L N.]]
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[[Category: D'Argenio DA]]
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[[Category: Valley, M P.]]
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[[Category: Lipscomb JD]]
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[[Category: Vetting, M W.]]
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[[Category: Ohlendorf DH]]
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[[Category: Aromatic degradation]]
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[[Category: Ornston LN]]
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[[Category: Beta-sandwich]]
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[[Category: Valley MP]]
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[[Category: Dioxygenase]]
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[[Category: Vetting MW]]
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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://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:49:53 2008''
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Current revision

Crystal Structure Of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S in Complex with Protocatechuate

PDB ID 2buv

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