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| - | ==STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNI== | + | |
| - | <StructureSection load='2jbr' size='340' side='right' caption='[[2jbr]], [[Resolution|resolution]] 2.30Å' scene=''> | + | ==Structure of the monooxygenase component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumanni== |
| | + | <StructureSection load='2jbr' size='340' side='right'caption='[[2jbr]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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]. <br> | + | <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> |
| - | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr><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> | + | <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> |
| | + | == Function == |
| | + | [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> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/2jbr_consurf.spt"</scriptWhenChecked> | + | <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> |
| - | </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]. | + | </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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| | Structure of the monooxygenase component of a two-component flavoprotein monooxygenase.,Alfieri A, Fersini F, Ruangchan N, Prongjit M, Chaiyen P, Mattevi A Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1177-82. Epub 2007 Jan 16. PMID:17227849<ref>PMID:17227849</ref> | | Structure of the monooxygenase component of a two-component flavoprotein monooxygenase.,Alfieri A, Fersini F, Ruangchan N, Prongjit M, Chaiyen P, Mattevi A Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1177-82. Epub 2007 Jan 16. PMID:17227849<ref>PMID:17227849</ref> |
| | | | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <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]] |
| - | [[Category: Alfieri, A.]] | + | [[Category: Large Structures]] |
| - | [[Category: Mattevi, A.]] | + | [[Category: Alfieri A]] |
| - | [[Category: Flavoenzyme hydroxylase]] | + | [[Category: Mattevi A]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii is a two-component system consisting of a NADH-dependent FMN reductase and a monooxygenase (C2) that uses reduced FMN as substrate. The crystal structures of C2 in the ligand-free and substrate-bound forms reveal a preorganized pocket that binds reduced FMN without large conformational changes. The Phe-266 side chain swings out to provide the space for binding p-hydroxyphenylacetate that is oriented orthogonal to the flavin ring. The geometry of the substrate-binding site of C2 is significantly different from that of p-hydroxybenzoate hydroxylase, a single-component flavoenzyme that catalyzes a similar reaction. The C2 overall structure resembles the folding of medium-chain acyl-CoA dehydrogenase. An outstanding feature in the C2 structure is a cavity located in front of reduced FMN; it has a spherical shape with a 1.9-A radius and a 29-A3 volume and is interposed between the flavin C4a atom and the substrate atom to be hydroxylated. The shape and position of this cavity are perfectly fit for housing the oxygen atoms of the flavin C4a-hydroperoxide intermediate that is formed upon reaction of the C2-bound reduced flavin with molecular oxygen. The side chain of His-396 is predicted to act as a hydrogen-bond donor to the oxygen atoms of the intermediate. This architecture promotes the nucleophilic attack of the substrate onto the terminal oxygen of the hydroperoxyflavin. Comparative analysis with the structures of other flavoenzymes indicates that a distinctive feature of monooxygenases is the presence of specific cavities that encapsulate and stabilize the crucial hydroperoxyflavin intermediate.
Structure of the monooxygenase component of a two-component flavoprotein monooxygenase.,Alfieri A, Fersini F, Ruangchan N, Prongjit M, Chaiyen P, Mattevi A Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1177-82. Epub 2007 Jan 16. PMID:17227849[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chaiyen P, Suadee C, Wilairat P. A novel two-protein component flavoprotein hydroxylase. Eur J Biochem. 2001 Nov;268(21):5550-61. PMID:11683878
- ↑ Thotsaporn K, Sucharitakul J, Wongratana J, Suadee C, Chaiyen P. Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases. Biochim Biophys Acta. 2004 Oct 5;1680(1):60-6. PMID:15451173 doi:http://dx.doi.org/10.1016/j.bbaexp.2004.08.003
- ↑ Sucharitakul J, Chaiyen P, Entsch B, Ballou DP. The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis. Biochemistry. 2005 Aug 2;44(30):10434-42. PMID:16042421 doi:http://dx.doi.org/10.1021/bi050615e
- ↑ Sucharitakul J, Chaiyen P, Entsch B, Ballou DP. Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii. J Biol Chem. 2006 Jun 23;281(25):17044-53. Epub 2006 Apr 20. PMID:16627482 doi:http://dx.doi.org/10.1074/jbc.M512385200
- ↑ Sucharitakul J, Phongsak T, Entsch B, Svasti J, Chaiyen P, Ballou DP. Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase. Biochemistry. 2007 Jul 24;46(29):8611-23. Epub 2007 Jun 27. PMID:17595116 doi:http://dx.doi.org/10.1021/bi7006614
- ↑ Ruangchan N, Tongsook C, Sucharitakul J, Chaiyen P. pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase. J Biol Chem. 2011 Jan 7;286(1):223-33. doi: 10.1074/jbc.M110.163881. Epub 2010, Oct 28. PMID:21030590 doi:http://dx.doi.org/10.1074/jbc.M110.163881
- ↑ Alfieri A, Fersini F, Ruangchan N, Prongjit M, Chaiyen P, Mattevi A. Structure of the monooxygenase component of a two-component flavoprotein monooxygenase. Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1177-82. Epub 2007 Jan 16. PMID:17227849
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