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2jbr

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==STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNI==
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<StructureSection load='2jbr' size='340' side='right' caption='[[2jbr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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==Structure of the monooxygenase component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumanni==
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<StructureSection load='2jbr' size='340' side='right'caption='[[2jbr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2jbr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JBR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2jbr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JBR FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jbr RCSB], [http://www.ebi.ac.uk/pdbsum/2jbr PDBsum]</span></td></tr>
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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]] 2.3&#8491;</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=2jbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbr OCA], [https://pdbe.org/2jbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jbr RCSB], [https://www.ebi.ac.uk/pdbsum/2jbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jbr ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HPAH_ACIBA HPAH_ACIBA] Oxygenase component of a two-component system that utilizes reduced FMN (FMNH2) supplied by the reductase component to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetate (3,4-DHPA). Also utilizes other reduced flavins such as FADH2 and reduced riboflavin to a lesser extent. Only the compounds with a hydroxyl group in the para (p-) position can be hydroxylated. May also oxidize phenol to catechol, and hydroxylate other phenol derivatives.<ref>PMID:11683878</ref> <ref>PMID:15451173</ref> <ref>PMID:16042421</ref> <ref>PMID:16627482</ref> <ref>PMID:17595116</ref> <ref>PMID:21030590</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/2jbr_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/2jbr_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2jbr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2jbr" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Acinetobacter baumannii]]
[[Category: Acinetobacter baumannii]]
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[[Category: Alfieri, A]]
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[[Category: Large Structures]]
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[[Category: Mattevi, A]]
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[[Category: Alfieri A]]
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[[Category: Flavoenzyme hydroxylase]]
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[[Category: Mattevi A]]
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[[Category: Oxidoreductase]]
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Current revision

Structure of the monooxygenase component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumanni

PDB ID 2jbr

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