2v3a: Difference between revisions

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<StructureSection load='2v3a' size='340' side='right'caption='[[2v3a]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2v3a' size='340' side='right'caption='[[2v3a]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2v3a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V3A FirstGlance]. <br>
<table><tr><td colspan='2'>[[2v3a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V3A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v3b|2v3b]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=2v3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3a OCA], [https://pdbe.org/2v3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v3a RCSB], [https://www.ebi.ac.uk/pdbsum/2v3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v3a 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=2v3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3a OCA], [https://pdbe.org/2v3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v3a RCSB], [https://www.ebi.ac.uk/pdbsum/2v3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v3a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RURE_PSEAE RURE_PSEAE]] Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.<ref>PMID:14574114</ref> <ref>PMID:12730186</ref>
[https://www.uniprot.org/uniprot/RURE_PSEAE RURE_PSEAE] Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.<ref>PMID:14574114</ref> <ref>PMID:12730186</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pseae]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Adams, T M]]
[[Category: Adams TM]]
[[Category: Hagelueken, G]]
[[Category: Hagelueken G]]
[[Category: Heinz, D W]]
[[Category: Heinz DW]]
[[Category: Kolmar, H]]
[[Category: Kolmar H]]
[[Category: Schubert, W D]]
[[Category: Schubert W-D]]
[[Category: Tuemmler, B]]
[[Category: Tuemmler B]]
[[Category: Wiehlmann, L]]
[[Category: Wiehlmann L]]
[[Category: Alkane degradation]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Nad]]
[[Category: Nadh oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Rubredoxin reductase]]

Latest revision as of 18:04, 13 December 2023

Crystal structure of rubredoxin reductase from Pseudomonas aeruginosa.Crystal structure of rubredoxin reductase from Pseudomonas aeruginosa.

Structural highlights

2v3a is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RURE_PSEAE Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.[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

Crude oil spills represent a major ecological threat because of the chemical inertness of the constituent n-alkanes. The Gram-negative bacterium Pseudomonas aeruginosa is one of the few bacterial species able to metabolize such compounds. Three chromosomal genes, rubB, rubA1, and rubA2 coding for an NAD(P)H:rubredoxin reductase (RdxR) and two rubredoxins (Rdxs) are indispensable for this ability. They constitute an electron transport (ET) pathway that shuttles reducing equivalents from carbon metabolism to the membrane-bound alkane hydroxylases AlkB1 and AlkB2. The RdxR-Rdx system also is crucial as part of the oxidative stress response in archaea or anaerobic bacteria. The redox couple has been analyzed in detail as a model system for ET processes. We have solved the structure of RdxR of P. aeruginosa both alone and in complex with Rdx, without the need for cross-linking, and both structures were refined at 2.40- and 2.45-A resolution, respectively. RdxR consists of two cofactor-binding domains and a C-terminal domain essential for the specific recognition of Rdx. Only a small number of direct interactions govern mutual recognition of RdxR and Rdx, corroborating the transient nature of the complex. The shortest distance between the redox centers is observed to be 6.2 A.

Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa.,Hagelueken G, Wiehlmann L, Adams TM, Kolmar H, Heinz DW, Tummler B, Schubert WD Proc Natl Acad Sci U S A. 2007 Jul 24;104(30):12276-81. Epub 2007 Jul 16. PMID:17636129[3]

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

References

  1. Smits TH, Witholt B, van Beilen JB. Functional characterization of genes involved in alkane oxidation by Pseudomonas aeruginosa. Antonie Van Leeuwenhoek. 2003;84(3):193-200. PMID:14574114
  2. Marin MM, Yuste L, Rojo F. Differential expression of the components of the two alkane hydroxylases from Pseudomonas aeruginosa. J Bacteriol. 2003 May;185(10):3232-7. PMID:12730186
  3. Hagelueken G, Wiehlmann L, Adams TM, Kolmar H, Heinz DW, Tummler B, Schubert WD. Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Proc Natl Acad Sci U S A. 2007 Jul 24;104(30):12276-81. Epub 2007 Jul 16. PMID:17636129

2v3a, resolution 2.40Å

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