1z03

From Proteopedia

(Difference between revisions)

Revision as of 06:26, 22 April 2020

2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction

Structural highlights

1z03 is a 6 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	2-hydroxyquinoline 8-monooxygenase, with EC number 1.14.13.61
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

2-Oxoquinoline 8-monooxygenase is a Rieske non-heme iron oxygenase that catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline in the soil bacterium Pseudomonas putida 86. The crystal structure of the oxygenase component of 2-oxoquinoline 8-monooxygenase shows a ring-shaped, C3-symmetric arrangement in which the mononuclear Fe(II) ion active site of one monomer is at a distance of 13 A from the Rieske-[2Fe-2S] center of a second monomer. Structural analyses of oxidized, reduced, and substrate bound states reveal the molecular bases for a new function of Fe-S clusters. Reduction of the Rieske center modulates the mononuclear Fe through a chain of conformational changes across the subunit interface, resulting in the displacement of Fe and its histidine ligand away from the substrate binding site. This creates an additional coordination site at the mononuclear Fe(II) ion and can open a pathway for dioxygen to bind in the substrate-containing active site.

2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction.,Martins BM, Svetlitchnaia T, Dobbek H Structure. 2005 May;13(5):817-24. PMID:15893671^[1]

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

References

↑ Martins BM, Svetlitchnaia T, Dobbek H. 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. Structure. 2005 May;13(5):817-24. PMID:15893671 doi:10.1016/j.str.2005.03.008

1 Structural highlights
2 Evolutionary Conservation
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/1z03"

@@ Line 1: / Line 1: @@
 ==2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction==
-<StructureSection load='1z03' size='340' side='right' caption='[[1z03]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1z03' size='340' side='right'caption='[[1z03]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z03]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z03 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z03]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z03 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z03 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OCH:QUINOLIN-2(1H)-ONE'>OCH</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OCH:QUINOLIN-2(1H)-ONE'>OCH</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-hydroxyquinoline_8-monooxygenase 2-hydroxyquinoline 8-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.61 1.14.13.61] </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=1z03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z03 OCA], [http://pdbe.org/1z03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z03 RCSB], [http://www.ebi.ac.uk/pdbsum/1z03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z03 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z03 OCA], [http://pdbe.org/1z03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z03 RCSB], [http://www.ebi.ac.uk/pdbsum/1z03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z03 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 32: / Line 32: @@
 </StructureSection>
 [[Category: 2-hydroxyquinoline 8-monooxygenase]]
+[[Category: Large Structures]]
 [[Category: Pseudomonas putida]]
 [[Category: Dobbek, H]]

1z03

From Proteopedia

Revision as of 06:26, 22 April 2020

2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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