2wj4

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(Difference between revisions)

Revision as of 06:22, 5 August 2016

CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER NITROGUAJACOLICUS RU61A ANAEROBICALLY COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4-OXOQUINALDINE

Structural highlights

2wj4 is a 4 chain structure with sequence from Artnt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	2wm2, 2wj3, 2wj6
Activity:	3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, with EC number 1.13.11.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HOD_ARTNT] Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.^[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

Enzymatic catalysis of oxygenation reactions in the absence of metal or organic cofactors is a considerable biochemical challenge. The CO-forming 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus Ru61a and 1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) from Pseudomonas putida 33/1 are homologous cofactor-independent dioxygenases involved in the breakdown of N-heteroaromatic compounds. To date, they are the only dioxygenases suggested to belong to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions. We present here the crystal structures of both HOD and QDO in their native state as well as the structure of HOD in complex with its natural 1-H-3-hydroxy-4-oxoquinaldine substrate, its N-acetylanthranilate reaction product, and chloride as dioxygen mimic. HOD and QDO are structurally very similar. They possess a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The "oxyanion hole" of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism. Our analysis provides a framework to explain cofactor-independent dioxygenation within a protein architecture generally employed to catalyze hydrolytic reactions.

Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold.,Steiner RA, Janssen HJ, Roversi P, Oakley AJ, Fetzner S Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):657-62. Epub 2009 Dec 22. PMID:20080731^[2]

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

References

↑ Betz A, Facey SJ, Hauer B, Tshisuaka B, Lingens F. Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Ru61a. J Basic Microbiol. 2000;40(1):7-23. PMID:10746195
↑ Steiner RA, Janssen HJ, Roversi P, Oakley AJ, Fetzner S. Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold. Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):657-62. Epub 2009 Dec 22. PMID:20080731

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/2wj4"

Categories: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase | Artnt | Steiner, R A | Alpha/beta hydrolase | Oxidoreductase

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER NITROGUAJACOLICUS RU61A ANAEROBICALLY COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4-OXOQUINALDINE==
 <StructureSection load='2wj4' size='340' side='right' caption='[[2wj4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wj4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_nitroguajacolicus Arthrobacter nitroguajacolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WJ4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wj4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Artnt Artnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WJ4 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HQD:3-HYDROXY-2-METHYLQUINOLIN-4(1H)-ONE'>HQD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wm2|2wm2]], [[2wj3|2wj3]], [[2wj6|2wj6]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxy-2-methylquinolin-4-one_2,4-dioxygenase 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.48 1.13.11.48] </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=2wj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wj4 RCSB], [http://www.ebi.ac.uk/pdbsum/2wj4 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=2wj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wj4 OCA], [http://pdbe.org/2wj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wj4 RCSB], [http://www.ebi.ac.uk/pdbsum/2wj4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wj4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A4V8M9_9MICC A4V8M9_9MICC]] Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.<ref>PMID:10746195</ref>
+[[http://www.uniprot.org/uniprot/HOD_ARTNT HOD_ARTNT]] Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.<ref>PMID:10746195</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wj4 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2wj4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 33: / Line 35: @@
 </StructureSection>
 [[Category: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase]]
-[[Category: Arthrobacter nitroguajacolicus]]
+[[Category: Artnt]]
 [[Category: Steiner, R A]]
 [[Category: Alpha/beta hydrolase]]
 [[Category: Oxidoreductase]]

2wj4

From Proteopedia

Revision as of 06:22, 5 August 2016

CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER NITROGUAJACOLICUS RU61A ANAEROBICALLY COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4-OXOQUINALDINE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

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