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3nbb

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Current revision

Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha

Structural highlights

3nbb is a 6 chain structure with sequence from Ogataea angusta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.05Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMO_PICAN

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 copper amine oxidases carry out two copper-dependent processes: production of their own redox-active cofactor (2,4,5-trihydroxyphenylalanine quinone, TPQ) and the subsequent oxidative deamination of substrate amines. Because the same active site pocket must facilitate both reactions, individual active site residues may serve multiple roles. We have examined the roles of a strictly conserved active site tyrosine Y305 in the copper amine oxidase from Hansenula polymorpha kinetically, spetroscopically (Dubois and Klinman (2006) Biochemistry 45, 3178), and, in the present work, structurally. While the Y305A enzyme is almost identical to the wild type, a novel, highly oxygenated species replaces TPQ in the Y305F active sites. This new structure not only provides the first direct detection of peroxy intermediates in cofactor biogenesis but also indicates the critical control of oxidation chemistry that can be conferred by a single active site residue.

Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.,Chen ZW, Datta S, Dubois JL, Klinman JP, Mathews FS Biochemistry. 2010 Aug 31;49(34):7393-402. PMID:20684524^[1]

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

References

↑ Chen ZW, Datta S, Dubois JL, Klinman JP, Mathews FS. Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity. Biochemistry. 2010 Aug 31;49(34):7393-402. PMID:20684524 doi:10.1021/bi100643y

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/3nbb"

@@ Line 3: / Line 3: @@
 <StructureSection load='3nbb' size='340' side='right'caption='[[3nbb]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nbb]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NBB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nbb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ogataea_angusta Ogataea angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NBB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2.05&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ME0:HYDROXY-L-METHIONINE'>ME0</scene>, <scene name='pdbligand=TY8:2,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY8</scene>, <scene name='pdbligand=TY9:3,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY9</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ME0:HYDROXY-L-METHIONINE'>ME0</scene>, <scene name='pdbligand=TY8:2,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY8</scene>, <scene name='pdbligand=TY9:3,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY9</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2v|1a2v]]</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=3nbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbb OCA], [https://pdbe.org/3nbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nbb RCSB], [https://www.ebi.ac.uk/pdbsum/3nbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbb ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Primary-amine_oxidase Primary-amine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 1.4.3.21] </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=3nbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbb OCA], [http://pdbe.org/3nbb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nbb RCSB], [http://www.ebi.ac.uk/pdbsum/3nbb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbb ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/AMO_PICAN AMO_PICAN]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Primary-amine oxidase]]
+[[Category: Ogataea angusta]]
-[[Category: Chen, Z]]
+[[Category: Chen Z]]
-[[Category: Datta, S]]
+[[Category: Datta S]]
-[[Category: DuBois, J L]]
+[[Category: DuBois JL]]
-[[Category: Klinman, J P]]
+[[Category: Klinman JP]]
-[[Category: Mathews, F S]]
+[[Category: Mathews FS]]
-[[Category: Amine oxidase]]
-[[Category: Oxidoreductase]]
-[[Category: Quinoprotein]]

3nbb

From Proteopedia

Current revision

Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha

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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