3lb8

From Proteopedia

(Difference between revisions)

Revision as of 08:34, 6 September 2023

Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex

Structural highlights

3lb8 is a 4 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAMA_PSEPU The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.^[1]

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

In the camphor monooxygenase system from Pseudomonas putida, the [2Fe-2S]-containing putidaredoxin (Pdx) shuttles electrons between the NADH-dependent putidaredoxin reductase (Pdr) and cytochrome P450(cam). The mechanism of the Pdr.Pdx redox couple has been investigated by a variety of techniques. One of the exceptions is x-ray crystallography as the native partners associate weakly and resist co-crystallization. Here, we present the 2.6-A x-ray structure of a catalytically active complex between Pdr and Pdx C73S/C85S chemically cross-linked via the Lys(409Pdr)-Glu(72Pdx) pair. The 365 A(2) Pdr-Pdx interface is predominantly hydrophobic with one central Arg(310Pdr)-Asp(38Pdx) salt bridge, likely assisting docking and orienting the partners optimally for electron transfer, and a few peripheral hydrogen bonds. A predicted 12-A-long electron transfer route between FAD and [2Fe-2S] includes flavin flanking Trp(330Pdr) and the iron ligand Cys(39Pdx). The x-ray model agrees well with the experimental and theoretical results and suggests that the linked Pdx must undergo complex movements during turnover to accommodate P450(cam), which could limit the Pdx-to-P450(cam) electron transfer reaction.

Crystal structure of the putidaredoxin reductase x putidaredoxin electron transfer complex.,Sevrioukova IF, Poulos TL, Churbanova IY J Biol Chem. 2010 Apr 30;285(18):13616-20. Epub 2010 Feb 23. PMID:20179327^[2]

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

References

↑ Sevrioukova IF, Poulos TL. Putidaredoxin reductase, a new function for an old protein. J Biol Chem. 2002 Jul 12;277(28):25831-9. Epub 2002 May 13. PMID:12011076 doi:http://dx.doi.org/10.1074/jbc.M201110200
↑ Sevrioukova IF, Poulos TL, Churbanova IY. Crystal structure of the putidaredoxin reductase x putidaredoxin electron transfer complex. J Biol Chem. 2010 Apr 30;285(18):13616-20. Epub 2010 Feb 23. PMID:20179327 doi:10.1074/jbc.M110.104968

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/3lb8"

Categories: Large Structures | Pseudomonas putida | Sevrioukova IF

@@ Line 3: / Line 3: @@
 <StructureSection load='3lb8' size='340' side='right'caption='[[3lb8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lb8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LB8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3lb8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LB8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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]] 2.6&#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;'>[[1q1r|1q1r]], [[1oqq|1oqq]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">camA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camA, camB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</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=3lb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lb8 OCA], [https://pdbe.org/3lb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lb8 RCSB], [https://www.ebi.ac.uk/pdbsum/3lb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lb8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CAMA_PSEPU CAMA_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.<ref>PMID:12011076</ref>  [[https://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
+[https://www.uniprot.org/uniprot/CAMA_PSEPU CAMA_PSEPU] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.<ref>PMID:12011076</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus fluorescens putidus flugge 1886]]
 [[Category: Large Structures]]
-[[Category: Sevrioukova, I F]]
+[[Category: Pseudomonas putida]]
-[[Category: Covalently linked protein-protein complex]]
+[[Category: Sevrioukova IF]]
-[[Category: Electron transport]]
-[[Category: Fad]]
-[[Category: Flavoprotein]]
-[[Category: Iron-sulfur]]
-[[Category: Metal-binding]]
-[[Category: Oxidoreductase]]
-[[Category: Oxidoreductase-electron transport complex]]

3lb8

From Proteopedia

Revision as of 08:34, 6 September 2023

Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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