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1t3q

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Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

Structural highlights

1t3q 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.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

P72223_PSEPU

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

The soil bacterium Pseudomonas putida 86 uses quinoline as a sole source of carbon and energy. Quinoline 2-oxidoreductase (Qor) catalyzes the first metabolic step converting quinoline to 2-oxo-1,2-dihydroquinoline. Qor is a member of the molybdenum hydroxylases. The molybdenum ion is coordinated by two ene-dithiolate sulfur atoms, two oxo-ligands, and a catalytically crucial sulfido-ligand, whose position in the active site was controversial. The 1.8 A resolution crystal structure of Qor indicates that the sulfido-ligand occupies the equatorial position at the molybdenum ion. The structural comparison of Qor with the allopurinol-inhibited xanthine dehydrogenase from Rhodobacter capsulatus allows direct insight into the mechanism of substrate recognition and the identification of putative catalytic residues. The active site protein variants QorE743V and QorE743D were analyzed to assess the catalytic role of E743.

Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.,Bonin I, Martins BM, Purvanov V, Fetzner S, Huber R, Dobbek H Structure. 2004 Aug;12(8):1425-35. PMID:15296736^[1]

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

References

↑ Bonin I, Martins BM, Purvanov V, Fetzner S, Huber R, Dobbek H. Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase. Structure. 2004 Aug;12(8):1425-35. PMID:15296736 doi:10.1016/j.str.2004.05.014

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t3q"

@@ Line 3: / Line 3: @@
 <StructureSection load='1t3q' size='340' side='right'caption='[[1t3q]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1t3q]] is a 6 chain structure with sequence from [http://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=1T3Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T3Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1t3q]] is a 6 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=1T3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T3Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCN:PTERIN+CYTOSINE+DINUCLEOTIDE'>MCN</scene>, <scene name='pdbligand=SMO:DIOXOSULFIDOMOLYBDENUM(VI)+ION'>SMO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quinoline_2-oxidoreductase Quinoline 2-oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.17 1.3.99.17] </span></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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCN:PTERIN+CYTOSINE+DINUCLEOTIDE'>MCN</scene>, <scene name='pdbligand=SMO:DIOXOSULFIDOMOLYBDENUM(VI)+ION'>SMO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1t3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3q OCA], [http://pdbe.org/1t3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t3q RCSB], [http://www.ebi.ac.uk/pdbsum/1t3q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3q 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=1t3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3q OCA], [https://pdbe.org/1t3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t3q RCSB], [https://www.ebi.ac.uk/pdbsum/1t3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3q ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/P72223_PSEPU P72223_PSEPU]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus fluorescens putidus flugge 1886]]
 [[Category: Large Structures]]
-[[Category: Quinoline 2-oxidoreductase]]
+[[Category: Pseudomonas putida]]
-[[Category: Bonin, I]]
+[[Category: Bonin I]]
-[[Category: Dobbek, H]]
+[[Category: Dobbek H]]
-[[Category: Fetzner, S]]
+[[Category: Fetzner S]]
-[[Category: Huber, R]]
+[[Category: Huber R]]
-[[Category: Martins, B M]]
+[[Category: Martins BM]]
-[[Category: Purvanov, V]]
+[[Category: Purvanov V]]
-[[Category: Mcd]]
-[[Category: Molybdenum]]
-[[Category: Oxidoreductase]]
-[[Category: Qor]]

1t3q

From Proteopedia

Current revision

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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