4d02

From Proteopedia

(Difference between revisions)

Revision as of 16:45, 5 August 2016

The crystallographic structure of Flavorubredoxin from Escherichia coli

Structural highlights

4d02 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NORV_ECOLI] Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase.^[1] ^[2]

Publication Abstract from PubMed

Flavodiiron proteins (FDPs) are a family of enzymes endowed with bona fide oxygen- and/or nitric oxide-reductase activity, although their substrate specificity determinants remain elusive. After a comprehensive comparison of available three-dimensional structures, particularly of FDPs with a clear preference towards either O2 or NO, two main differences were identified near the diiron active site, which led to the construction of site-directed mutants of Y271 and K53 in the oxygen reducing Entamoeba histolytica EhFdp1. The biochemical and biophysical properties of these mutants were studied by UV-visible and electron paramagnetic resonance (EPR) spectroscopies coupled to potentiometry. Their reactivity with O2 and NO was analyzed by stopped-flow absorption spectroscopy and amperometric methods. These mutations, while keeping the overall properties of the redox cofactors, resulted in increased NO reductase activity and faster inactivation of the enzyme in the reaction with O2, pointing to a role of the mutated residues in substrate selectivity.

Flavodiiron oxygen reductase from Entamoeba histolytica: Modulation of substrate preference by tyrosine 271 and lysine 53.,Goncalves VL, Vicente JB, Pinto L, Romao CV, Frazao C, Sarti P, Giuffre A, Teixeira M J Biol Chem. 2014 Aug 23. pii: jbc.M114.579086. PMID:25151360^[3]

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

References

↑ Gardner AM, Helmick RA, Gardner PR. Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli. J Biol Chem. 2002 Mar 8;277(10):8172-7. Epub 2001 Dec 18. PMID:11751865 doi:http://dx.doi.org/10.1074/jbc.M110471200
↑ Gomes CM, Giuffre A, Forte E, Vicente JB, Saraiva LM, Brunori M, Teixeira M. A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin. J Biol Chem. 2002 Jul 12;277(28):25273-6. Epub 2002 May 6. PMID:12101220 doi:http://dx.doi.org/10.1074/jbc.M203886200
↑ Goncalves VL, Vicente JB, Pinto L, Romao CV, Frazao C, Sarti P, Giuffre A, Teixeira M. Flavodiiron oxygen reductase from Entamoeba histolytica: Modulation of substrate preference by tyrosine 271 and lysine 53. J Biol Chem. 2014 Aug 23. pii: jbc.M114.579086. PMID:25151360 doi:http://dx.doi.org/10.1074/jbc.M114.579086

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d02"

@@ Line 1: / Line 1: @@
 ==The crystallographic structure of Flavorubredoxin from Escherichia coli==
 <StructureSection load='4d02' size='340' side='right' caption='[[4d02]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4d02]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D02 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4d02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d02 RCSB], [http://www.ebi.ac.uk/pdbsum/4d02 PDBsum]</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=4d02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d02 OCA], [http://pdbe.org/4d02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d02 RCSB], [http://www.ebi.ac.uk/pdbsum/4d02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d02 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4d02" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4d02

From Proteopedia

Revision as of 16:45, 5 August 2016

The crystallographic structure of Flavorubredoxin from Escherichia coli

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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