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[[Image:2but.gif|left|200px]]
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{{STRUCTURE_2but|  PDB=2but  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 MUTANT R457S- APO'''


==Crystal Structure Of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S - APO==
<StructureSection load='2but' size='340' side='right'caption='[[2but]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2but]] 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=2BUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2but FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2but OCA], [https://pdbe.org/2but PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2but RCSB], [https://www.ebi.ac.uk/pdbsum/2but PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2but ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== 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/bu/2but_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=2but ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2BUT 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=2BUT OCA].
</div>
<div class="pdbe-citations 2but" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
[[Category: Acinetobacter calcoaceticus]]
== References ==
[[Category: Protein complex]]
<references/>
[[Category: Protocatechuate 3,4-dioxygenase]]
__TOC__
[[Category: Argenio, D A.D.]]
</StructureSection>
[[Category: Lipscomb, J D.]]
[[Category: Acinetobacter baylyi ADP1]]
[[Category: Ohlendorf, D H.]]
[[Category: Large Structures]]
[[Category: Ornston, L N.]]
[[Category: D'Argenio DA]]
[[Category: Valley, M P.]]
[[Category: Lipscomb JD]]
[[Category: Vetting, M W.]]
[[Category: Ohlendorf DH]]
[[Category: Aromatic degradation]]
[[Category: Ornston LN]]
[[Category: Aromatic hydrocarbons catabolism]]
[[Category: Valley MP]]
[[Category: Dioxygenase]]
[[Category: Vetting MW]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Non-heme iron]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:49:48 2008''

Latest revision as of 13:56, 13 December 2023

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

2but, resolution 1.85Å

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