Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa.

2.50
Hdl Handle:
http://hdl.handle.net/10033/19758
Title:
Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa.
Authors:
Hagelueken, Gregor; Wiehlmann, Lutz; Adams, Thorsten M; Kolmar, Harald; Heinz, Dirk W; Tümmler, Burkhard; Schubert, Wolf-Dieter
Abstract:
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.
Affiliation:
Molecular Host-Pathogen Interactions, Division of Structural Biology, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
Citation:
Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. 2007, 104 (30):12276-81 Proc. Natl. Acad. Sci. U.S.A.
Journal:
Proceedings of the National Academy of Sciences of the United States of America
Issue Date:
24-Jul-2007
URI:
http://hdl.handle.net/10033/19758
DOI:
10.1073/pnas.0702919104
PubMed ID:
17636129
Type:
Article
Language:
en
ISSN:
0027-8424
Appears in Collections:
Publications from Division of Molekulare Struktur Biologie (MOSB)

Full metadata record

DC FieldValue Language
dc.contributor.authorHagelueken, Gregor-
dc.contributor.authorWiehlmann, Lutz-
dc.contributor.authorAdams, Thorsten M-
dc.contributor.authorKolmar, Harald-
dc.contributor.authorHeinz, Dirk W-
dc.contributor.authorTümmler, Burkhard-
dc.contributor.authorSchubert, Wolf-Dieter-
dc.date.accessioned2008-03-05T10:23:42Z-
dc.date.available2008-03-05T10:23:42Z-
dc.date.issued2007-07-24-
dc.identifier.citationCrystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. 2007, 104 (30):12276-81 Proc. Natl. Acad. Sci. U.S.A.en
dc.identifier.issn0027-8424-
dc.identifier.pmid17636129-
dc.identifier.doi10.1073/pnas.0702919104-
dc.identifier.urihttp://hdl.handle.net/10033/19758-
dc.description.abstractCrude 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.en
dc.language.isoenen
dc.subject.meshAlkanesen
dc.subject.meshBinding Sitesen
dc.subject.meshCrystallography, X-Rayen
dc.subject.meshDimerizationen
dc.subject.meshElectronsen
dc.subject.meshElectrostaticsen
dc.subject.meshFlavin-Adenine Dinucleotideen
dc.subject.meshModels, Molecularen
dc.subject.meshNADH, NADPH Oxidoreductasesen
dc.subject.meshNADPen
dc.subject.meshNickelen
dc.subject.meshOxidation-Reductionen
dc.subject.meshPhylogenyen
dc.subject.meshProtein Bindingen
dc.subject.meshProtein Structure, Quaternaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshPseudomonas aeruginosaen
dc.subject.meshRubredoxinsen
dc.titleCrystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa.en
dc.typeArticleen
dc.contributor.departmentMolecular Host-Pathogen Interactions, Division of Structural Biology, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.en
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaen
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