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3k86

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Crystal structure of NADH:FAD oxidoreductase (TftC) - apo form

Structural highlights

3k86 is a 2 chain structure with sequence from Burkholderia cepacia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TFTC_BURCE Reductase component of a two-component system that degrades 2,4,5-trichlorophenol. TftC provides the FADH(2) required by TftD. 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.^[1] ^[2]

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

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gisi MR, Xun L. Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100. J Bacteriol. 2003 May;185(9):2786-92. PMID:12700257
↑ Webb BN, Ballinger JW, Kim E, Belchik SM, Lam KS, Youn B, Nissen MS, Xun L, Kang C. Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100. J Biol Chem. 2010 Jan 15;285(3):2014-27. Epub 2009 Nov 13. PMID:19915006 doi:10.1074/jbc.M109.056135
↑ Webb BN, Ballinger JW, Kim E, Belchik SM, Lam KS, Youn B, Nissen MS, Xun L, Kang C. Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100. J Biol Chem. 2010 Jan 15;285(3):2014-27. Epub 2009 Nov 13. PMID:19915006 doi:10.1074/jbc.M109.056135

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3k86"

Categories: Burkholderia cepacia | Large Structures | Kang CH | Webb BN

@@ Line 1: / Line 1: @@
 ==Crystal structure of NADH:FAD oxidoreductase (TftC) - apo form==
-<StructureSection load='3k86' size='340' side='right' caption='[[3k86]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3k86' size='340' side='right'caption='[[3k86]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3k86]] is a 2 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=3K86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K86 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3k86]] is a 2 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=3K86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K86 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k87|3k87]], [[3k88|3k88]]</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&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tftC ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3k86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k86 OCA], [https://pdbe.org/3k86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k86 RCSB], [https://www.ebi.ac.uk/pdbsum/3k86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k86 ProSAT]</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=3k86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k86 RCSB], [http://www.ebi.ac.uk/pdbsum/3k86 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/TFTC_BURCE TFTC_BURCE] Reductase component of a two-component system that degrades 2,4,5-trichlorophenol. TftC provides the FADH(2) required by TftD. 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.<ref>PMID:12700257</ref> <ref>PMID:19915006</ref>
 == 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/k8/3k86_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/3k86_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].
+</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=3k86 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3k86" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 == References ==
 <references/>
@@ Line 30: / Line 36: @@
 </StructureSection>
 [[Category: Burkholderia cepacia]]
-[[Category: Kang, C H]]
+[[Category: Large Structures]]
-[[Category: Webb, B N]]
+[[Category: Kang CH]]
-[[Category: Monooxygenase]]
+[[Category: Webb BN]]
-[[Category: Nadh:fad oxidoreductase]]
-[[Category: Oxidoreductase]]

3k86

From Proteopedia

Current revision

Crystal structure of NADH:FAD oxidoreductase (TftC) - apo form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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