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{{Seed}}
==CRYSTAL STRUCTURE OF THE CITROBACTER SP. TRIPHENYLMETHANE REDUCTASE COMPLEXED WITH NADP(H)==
[[Image:2vrb.png|left|200px]]
<StructureSection load='2vrb' size='340' side='right' caption='[[2vrb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vrb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Citrobacter_sp._my-5 Citrobacter sp. my-5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VRB FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jl1|2jl1]], [[2vrc|2vrc]]</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=2vrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vrb RCSB], [http://www.ebi.ac.uk/pdbsum/2vrb 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/vr/2vrb_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 ==
Triphenylmethane dyes are aromatic xenobiotic compounds that are widely considered to be one of the main culprits of environmental pollution. Triphenylmethane reductase (TMR) from Citrobacter sp. strain KCTC 18061P was initially isolated and biochemically characterized as an enzyme that catalyzes the reduction of triphenylmethane dyes. Information from the primary amino acid sequence suggests that TMR is a dinucleotide-binding motif-containing enzyme; however, no other functional clues can be derived from sequence analysis. We present the crystal structure of TMR in complex with NADP+ at 2.0-angstroms resolution. Despite limited sequence similarity, the enzyme shows remarkable structural similarity to short-chain dehydrogenase/reductase (SDR) family proteins. Functional assignments revealed that TMR has features of both classic and extended SDR family members and does not contain a conserved active site. Thus, it constitutes a novel class of SDR family proteins. On the basis of simulated molecular docking using the substrate malachite green and the TMR/NADP+ crystal structure, together with site-directed mutagenesis, we have elucidated a potential molecular mechanism for triphenylmethane dye reduction.


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Structural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase.,Kim MH, Kim Y, Park HJ, Lee JS, Kwak SN, Jung WH, Lee SG, Kim D, Lee YC, Oh TK J Biol Chem. 2008 Nov 14;283(46):31981-90. Epub 2008 Sep 9. PMID:18782772<ref>PMID:18782772</ref>
The line below this paragraph, containing "STRUCTURE_2vrb", creates the "Structure Box" on the page.
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{{STRUCTURE_2vrb|  PDB=2vrb  |  SCENE=  }}


===CRYSTAL STRUCTURE OF THE CITROBACTER SP. TRIPHENYLMETHANE REDUCTASE COMPLEXED WITH NADP(H)===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
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<references/>
The line below this paragraph, {{ABSTRACT_PUBMED_18782772}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 18782772 is the PubMed ID number.
</StructureSection>
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[[Category: Citrobacter sp. my-5]]
{{ABSTRACT_PUBMED_18782772}}
 
==About this Structure==
2VRB is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRB OCA].
 
==Reference==
<ref group="xtra">PMID:18782772</ref><references group="xtra"/>
[[Category: Bacteria]]
[[Category: Kim, M H.]]
[[Category: Kim, M H.]]
[[Category: Kim, Y.]]
[[Category: Kim, Y.]]
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[[Category: Sdr family]]
[[Category: Sdr family]]
[[Category: Triphenylmethane reduction]]
[[Category: Triphenylmethane reduction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:27:42 2009''

Revision as of 04:44, 1 October 2014

CRYSTAL STRUCTURE OF THE CITROBACTER SP. TRIPHENYLMETHANE REDUCTASE COMPLEXED WITH NADP(H)CRYSTAL STRUCTURE OF THE CITROBACTER SP. TRIPHENYLMETHANE REDUCTASE COMPLEXED WITH NADP(H)

Structural highlights

2vrb is a 1 chain structure with sequence from Citrobacter sp. my-5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:2jl1, 2vrc
Resources:FirstGlance, OCA, RCSB, PDBsum

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

Triphenylmethane dyes are aromatic xenobiotic compounds that are widely considered to be one of the main culprits of environmental pollution. Triphenylmethane reductase (TMR) from Citrobacter sp. strain KCTC 18061P was initially isolated and biochemically characterized as an enzyme that catalyzes the reduction of triphenylmethane dyes. Information from the primary amino acid sequence suggests that TMR is a dinucleotide-binding motif-containing enzyme; however, no other functional clues can be derived from sequence analysis. We present the crystal structure of TMR in complex with NADP+ at 2.0-angstroms resolution. Despite limited sequence similarity, the enzyme shows remarkable structural similarity to short-chain dehydrogenase/reductase (SDR) family proteins. Functional assignments revealed that TMR has features of both classic and extended SDR family members and does not contain a conserved active site. Thus, it constitutes a novel class of SDR family proteins. On the basis of simulated molecular docking using the substrate malachite green and the TMR/NADP+ crystal structure, together with site-directed mutagenesis, we have elucidated a potential molecular mechanism for triphenylmethane dye reduction.

Structural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase.,Kim MH, Kim Y, Park HJ, Lee JS, Kwak SN, Jung WH, Lee SG, Kim D, Lee YC, Oh TK J Biol Chem. 2008 Nov 14;283(46):31981-90. Epub 2008 Sep 9. PMID:18782772[1]

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

References

  1. ↑ Kim MH, Kim Y, Park HJ, Lee JS, Kwak SN, Jung WH, Lee SG, Kim D, Lee YC, Oh TK. Structural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase. J Biol Chem. 2008 Nov 14;283(46):31981-90. Epub 2008 Sep 9. PMID:18782772 doi:10.1074/jbc.M804092200

2vrb, resolution 2.00Å

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