3hwc - Revision history

OCA at 10:02, 21 February 2024

2024-02-21T10:02:01Z

←Older revision		Revision as of 10:02, 21 February 2024
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	<StructureSection load='3hwc' size='340' side='right'caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3hwc' size='340' side='right'caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"pseudomonas_cepacia"_burkholder_1950 "pseudomonas~~ cepacia~~" burkholder 1950~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HWC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HWC FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~tftD (~~[~~https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=~~5&~~id=292 "Pseudomonas cepacia" Burkholder 1950])~~</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]] 2.5Å</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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [https://pdbe.org/3hwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [https://www.ebi.ac.uk/pdbsum/3hwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hwc ProSAT]</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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [https://pdbe.org/3hwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [https://www.ebi.ac.uk/pdbsum/3hwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hwc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TFTD_BURCE TFTD_BURCE]] Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>	+	[https://www.uniprot.org/uniprot/TFTD_BURCE TFTD_BURCE] Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 19:
	</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=3hwc 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=3hwc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Burkholderia cepacia AC1100 completely degrades 2,4,5-trichlorophenol, in which an FADH(2)-dependent monooxygenase (TftD) and an NADH:FAD oxidoreductase (TftC) catalyze the initial steps. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone. In those processes, TftC provides all the required FADH(2). We have determined the crystal structures of dimeric TftC and tetrameric TftD at 2.0 and 2.5 A resolution, respectively. The structure of TftC was similar to those of related flavin reductases. The stacked nicotinamide:isoalloxazine rings in TftC and sequential reaction kinetics suggest that the reduced FAD leaves TftC after NADH oxidation. The structure of TftD was also similar to the known structures of FADH(2)-dependent monooxygenases. Its His-289 residue in the re-side of the isoalloxazine ring is within hydrogen bonding distance with a hydroxyl group of 2,5-DiCHQ. An H289A mutation resulted in the complete loss of activity toward 2,5-DiCHQ and a significant decrease in catalytic efficiency toward 2,4,5-TCP. Thus, His-289 plays different roles in the catalysis of 2,4,5-TCP and 2,5-DiCHQ. The results support that free FADH(2) is generated by TftC, and TftD uses FADH(2) to separately transform 2,4,5-TCP and 2,5-DiCHQ. Additional experimental data also support the diffusion of FADH(2) between TftC and TftD without direct physical interaction between the two enzymes.
-
-	Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100.,Webb BN, Ballinger JW, Kim E, Belchik SM, Lam KS, Youn B, Nissen MS, Xun L, Kang C J Biol Chem. 2010 Jan 15;285(3):2014-27. Epub 2009 Nov 13. PMID:19915006<ref>PMID:19915006</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3hwc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Pseudomonas~~ cepacia ~~burkholder 1950~~]]	+	[[Category: Burkholderia cepacia]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ballinger~~, J W~~]]	+	[[Category: Ballinger JW]]
-	[[Category: Kang~~, C H]]~~	+	[[Category: Kang CH]]
-	~~[[Category: Beta barrel]]~~	+
-	~~[[Category: Helix bundle]]~~	+
-	~~[[Category: Monooxygenase]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 11:59, 30 March 2022

2022-03-30T11:59:08Z

←Older revision		Revision as of 11:59, 30 March 2022
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	==Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100==		==Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100==
-	<StructureSection load='3hwc' size='340' side='right' caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='3hwc' size='340' side='right'caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3HWC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HWC FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tftD ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292 "Pseudomonas cepacia" Burkholder 1950])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tftD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292 "Pseudomonas cepacia" Burkholder 1950])</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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [~~http~~://pdbe.org/3hwc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3hwc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3hwc ProSAT]</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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [https://pdbe.org/3hwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [https://www.ebi.ac.uk/pdbsum/3hwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hwc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TFTD_BURCE TFTD_BURCE]] Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>	+	[[https://www.uniprot.org/uniprot/TFTD_BURCE TFTD_BURCE]] Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Monooxygenase\|Monooxygenase]]	+	*[[Monooxygenase 3D structures\|Monooxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Pseudomonas cepacia burkholder 1950]]		[[Category: Pseudomonas cepacia burkholder 1950]]
		+	[[Category: Large Structures]]
	[[Category: Ballinger, J W]]		[[Category: Ballinger, J W]]
	[[Category: Kang, C H]]		[[Category: Kang, C H]]

OCA at 07:57, 12 December 2018

2018-12-12T07:57:03Z

←Older revision		Revision as of 07:57, 12 December 2018
Line 1:		Line 1:
		+
	==Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100==		==Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100==
	<StructureSection load='3hwc' size='340' side='right' caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3hwc' size='340' side='right' caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HWC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HWC FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tftD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292 "Pseudomonas cepacia" Burkholder 1950])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tftD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292 "Pseudomonas cepacia" Burkholder 1950])</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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [http://pdbe.org/3hwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [http://www.ebi.ac.uk/pdbsum/3hwc PDBsum]</span></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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [http://pdbe.org/3hwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [http://www.ebi.ac.uk/pdbsum/3hwc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hwc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hw/3hwc_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hw/3hwc_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>
Line 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 3hwc" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3hwc" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Monooxygenase\|Monooxygenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:44, 7 February 2016

2016-02-07T04:44:56Z

←Older revision		Revision as of 04:44, 7 February 2016
Line 2:		Line 2:
	<StructureSection load='3hwc' size='340' side='right' caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3hwc' size='340' side='right' caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Burkholderia_cepacia Burkholderia~~ cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HWC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HWC FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tftD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292 ~~Burkholderia~~ cepacia])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tftD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292 "Pseudomonas cepacia" Burkholder 1950])</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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [http://www.ebi.ac.uk/pdbsum/3hwc PDBsum]</span></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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [http://pdbe.org/3hwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [http://www.ebi.ac.uk/pdbsum/3hwc PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~O87009_BURCE O87009_BURCE~~]] Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>	+	[[http://www.uniprot.org/uniprot/TFTD_BURCE TFTD_BURCE]] Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 16:		Line 16:
	<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=3hwc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 26:		Line 26:
	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 3hwc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Burkholderia~~ cepacia]]	+	[[Category: Pseudomonas cepacia burkholder 1950]]
	[[Category: Ballinger, J W]]		[[Category: Ballinger, J W]]
	[[Category: Kang, C H]]		[[Category: Kang, C H]]

OCA at 07:57, 24 December 2014

2014-12-24T07:57:12Z

←Older revision		Revision as of 07:57, 24 December 2014
Line 6:		Line 6:
	<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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [http://www.ebi.ac.uk/pdbsum/3hwc PDBsum]</span></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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [http://www.ebi.ac.uk/pdbsum/3hwc PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/O87009_BURCE O87009_BURCE]] Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:09, 8 December 2014

2014-12-08T09:09:09Z

←Older revision		Revision as of 09:09, 8 December 2014
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-	[[~~Image~~:3hwc.~~png\|left~~\|200px]]	+	==Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100==
		+	<StructureSection load='3hwc' size='340' side='right' caption='[[3hwc]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3hwc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HWC FirstGlance]. <br>
		+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tftD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=292 Burkholderia cepacia])</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=3hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hwc RCSB], [http://www.ebi.ac.uk/pdbsum/3hwc PDBsum]</span></td></tr>
		+	</table>
		+	== 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/hw/3hwc_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Burkholderia cepacia AC1100 completely degrades 2,4,5-trichlorophenol, in which an FADH(2)-dependent monooxygenase (TftD) and an NADH:FAD oxidoreductase (TftC) catalyze the initial steps. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone. In those processes, TftC provides all the required FADH(2). We have determined the crystal structures of dimeric TftC and tetrameric TftD at 2.0 and 2.5 A resolution, respectively. The structure of TftC was similar to those of related flavin reductases. The stacked nicotinamide:isoalloxazine rings in TftC and sequential reaction kinetics suggest that the reduced FAD leaves TftC after NADH oxidation. The structure of TftD was also similar to the known structures of FADH(2)-dependent monooxygenases. Its His-289 residue in the re-side of the isoalloxazine ring is within hydrogen bonding distance with a hydroxyl group of 2,5-DiCHQ. An H289A mutation resulted in the complete loss of activity toward 2,5-DiCHQ and a significant decrease in catalytic efficiency toward 2,4,5-TCP. Thus, His-289 plays different roles in the catalysis of 2,4,5-TCP and 2,5-DiCHQ. The results support that free FADH(2) is generated by TftC, and TftD uses FADH(2) to separately transform 2,4,5-TCP and 2,5-DiCHQ. Additional experimental data also support the diffusion of FADH(2) between TftC and TftD without direct physical interaction between the two enzymes.

-	~~{{STRUCTURE_3hwc\| PDB=3hwc \| SCENE= }}~~	+	Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100.,Webb BN, Ballinger JW, Kim E, Belchik SM, Lam KS, Youn B, Nissen MS, Xun L, Kang C J Biol Chem. 2010 Jan 15;285(3):2014-27. Epub 2009 Nov 13. PMID:19915006<ref>PMID:19915006</ref>

-	~~===Crystal Structure~~ of ~~Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_19915006}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[3hwc]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Burkholderia_cepacia Burkholderia cepacia]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:019915006<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Burkholderia cepacia]]		[[Category: Burkholderia cepacia]]
-	[[Category: Ballinger, J W.]]	+	[[Category: Ballinger, J W]]
-	[[Category: Kang, C H.]]	+	[[Category: Kang, C H]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
	[[Category: Helix bundle]]		[[Category: Helix bundle]]
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA: Protected "3hwc" [edit=sysop:move=sysop]

2013-03-06T15:02:45Z

Protected "3hwc" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:02, 6 March 2013

OCA at 15:02, 6 March 2013

2013-03-06T15:02:42Z

←Older revision		Revision as of 15:02, 6 March 2013
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-	{{Seed}}
	[[Image:3hwc.png\|left\|200px]]		[[Image:3hwc.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3hwc", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3hwc\| PDB=3hwc \| SCENE= }}		{{STRUCTURE_3hwc\| PDB=3hwc \| SCENE= }}

	===Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100===		===Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19915006}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19915006 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19915006}}		{{ABSTRACT_PUBMED_19915006}}

	==About this Structure==		==About this Structure==
-	~~3HWC~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA].	+	[[3hwc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19915006~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019915006</ref><references group="xtra"/>
	[[Category: Burkholderia cepacia]]		[[Category: Burkholderia cepacia]]
	[[Category: Ballinger, J W.]]		[[Category: Ballinger, J W.]]
Line 31:		Line 19:
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 3 14:37:17 2010''

OCA at 12:37, 3 March 2010

2010-03-03T12:37:19Z

←Older revision		Revision as of 12:37, 3 March 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3hwc.~~jpg~~\|left\|200px]]	+	[[Image:3hwc.png\|left\|200px]]

	<!--		<!--
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	===Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100===		===Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19915006}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19915006 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19915006}}

	==About this Structure==		==About this Structure==
-	3HWC is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA].	+	3HWC is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19915006</ref><references group="xtra"/>
	[[Category: Burkholderia cepacia]]		[[Category: Burkholderia cepacia]]
	[[Category: Ballinger, J W.]]		[[Category: Ballinger, J W.]]
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	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Nov 11 22~~:28:~~13 2009~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 3 14:37:17 2010''

OCA at 20:28, 11 November 2009

2009-11-11T20:28:17Z

←Older revision		Revision as of 20:28, 11 November 2009
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-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3hwc.jpg\|left\|200px]]

-	The ~~entry 3hwc~~ is ~~ON HOLD~~ ~~until Jun 17 2011~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3hwc", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3hwc\| PDB=3hwc \| SCENE= }}

-	~~Authors: Ballinger, J.W., Kang, C.H.~~	+	===Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100===

-	Description: Crystal Structure of Chlorophenol 4-Monooxygenase (TftD) of Burkholderia cepacia AC1100

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jul 1 08~~:57:04 2009''	+	==About this Structure==
		+	3HWC is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HWC OCA].
		+	[[Category: Burkholderia cepacia]]
		+	[[Category: Ballinger, J W.]]
		+	[[Category: Kang, C H.]]
		+	[[Category: Beta barrel]]
		+	[[Category: Helix bundle]]
		+	[[Category: Monooxygenase]]
		+	[[Category: Oxidoreductase]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 11 22:28:13 2009''