2yr4: Difference between revisions

Latest revision as of 13:54, 13 March 2024

Crystal structure of L-phenylalanine oxiase from Psuedomonas sp. P-501

Structural highlights

2yr4 is a 2 chain structure with sequence from Pseudomonas sp. P-501. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:	FAD, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAO_PSESP Catalyzes both oxygenative decarboxylation and oxidative deamination, depending on the substrate used. Has high activity for L-Phe and L-Tyr, but relatively low activities for L-Met and L-Trp. L-Phe is mainly oxygenated and L-Met is mainly oxidized.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Suzuki H, Higashi Y, Asano M, Suguro M, Kigawa M, Maeda M, Katayama S, Mukouyama EB, Uchiyama K. Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme. J Biochem. 2004 Nov;136(5):617-27. PMID:15632301 doi:10.1093/jb/mvh169
↑ Ohta Y, Mukouyama EB, Suzuki H. Kinetic isotope effect of the L-phenylalanine oxidase from Pseudomonas sp. P-501. J Biochem. 2006 Mar;139(3):551-5. PMID:16567420 doi:10.1093/jb/mvj049
↑ Koyama H, Suzuki H. Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating). J Biochem. 1986 Oct;100(4):859-66. PMID:3818566 doi:10.1093/oxfordjournals.jbchem.a121798
↑ Koyama H. Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1984 Aug;96(2):421-7. PMID:6501250 doi:10.1093/oxfordjournals.jbchem.a134853
↑ Koyama H. Further characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1983 May;93(5):1313-9. PMID:6885723 doi:10.1093/oxfordjournals.jbchem.a134265
↑ Koyama H. Purification and characterization of a novel L-phenylalanine oxidase (Deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1982 Oct;92(4):1235-40. PMID:7174643 doi:10.1093/oxfordjournals.jbchem.a134041

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OCA

[1] Suzuki H, Higashi Y, Asano M, Suguro M, Kigawa M, Maeda M, Katayama S, Mukouyama EB, Uchiyama K. Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme. J Biochem. 2004 Nov;136(5):617-27. PMID:15632301 doi:10.1093/jb/mvh169

[2] Ohta Y, Mukouyama EB, Suzuki H. Kinetic isotope effect of the L-phenylalanine oxidase from Pseudomonas sp. P-501. J Biochem. 2006 Mar;139(3):551-5. PMID:16567420 doi:10.1093/jb/mvj049

[3] Koyama H, Suzuki H. Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating). J Biochem. 1986 Oct;100(4):859-66. PMID:3818566 doi:10.1093/oxfordjournals.jbchem.a121798

[4] Koyama H. Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1984 Aug;96(2):421-7. PMID:6501250 doi:10.1093/oxfordjournals.jbchem.a134853

[5] Koyama H. Further characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1983 May;93(5):1313-9. PMID:6885723 doi:10.1093/oxfordjournals.jbchem.a134265

[6] Koyama H. Purification and characterization of a novel L-phenylalanine oxidase (Deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1982 Oct;92(4):1235-40. PMID:7174643 doi:10.1093/oxfordjournals.jbchem.a134041

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[2]

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[4]

[5]

[6]

@@ Line 1: / Line 1: @@
-[[Image:2yr4.jpg|left|200px]]
-<!--
+==Crystal structure of L-phenylalanine oxiase from Psuedomonas sp. P-501==
-The line below this paragraph, containing "STRUCTURE_2yr4", creates the "Structure Box" on the page.
+<StructureSection load='2yr4' size='340' side='right'caption='[[2yr4]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2yr4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._P-501 Pseudomonas sp. P-501]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YR4 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_2yr4|  PDB=2yr4  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yr4 OCA], [https://pdbe.org/2yr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yr4 RCSB], [https://www.ebi.ac.uk/pdbsum/2yr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yr4 ProSAT]</span></td></tr>
+</table>
-'''Crystal structure of L-phenylalanine oxiase from Psuedomonas sp. P-501'''
+== Function ==
+[https://www.uniprot.org/uniprot/PAO_PSESP PAO_PSESP] Catalyzes both oxygenative decarboxylation and oxidative deamination, depending on the substrate used. Has high activity for L-Phe and L-Tyr, but relatively low activities for L-Met and L-Trp. L-Phe is mainly oxygenated and L-Met is mainly oxidized.<ref>PMID:15632301</ref> <ref>PMID:16567420</ref> <ref>PMID:3818566</ref> <ref>PMID:6501250</ref> <ref>PMID:6885723</ref> <ref>PMID:7174643</ref>
+== Evolutionary Conservation ==
-==About this Structure==
+[[Image:Consurf_key_small.gif|200px|right]]
-YR4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YR4 OCA].
+Check<jmol>
-[[Category: Bacteria]]
+  <jmolCheckbox>
-[[Category: Phenylalanine 2-monooxygenase]]
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yr/2yr4_consurf.spt"</scriptWhenChecked>
-[[Category: Single protein]]
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-[[Category: Ida, K.]]
+    <text>to colour the structure by Evolutionary Conservation</text>
-[[Category: Kurabayashi, M.]]
+  </jmolCheckbox>
-[[Category: Suguro, M.]]
+</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=2yr4 ConSurf].
-[[Category: Suzuki, H.]]
+<div style="clear:both"></div>
-[[Category: Amino oxidase]]
+== References ==
-[[Category: Flavoenzyme]]
+<references/>
-[[Category: L-phenylalanine oxidase]]
+__TOC__
-[[Category: Oxidoreductase]]
+</StructureSection>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:08:18 2008''
+[[Category: Large Structures]]
+[[Category: Pseudomonas sp. P-501]]
+[[Category: Ida K]]
+[[Category: Kurabayashi M]]
+[[Category: Suguro M]]
+[[Category: Suzuki H]]

2yr4: Difference between revisions

Latest revision as of 13:54, 13 March 2024

Crystal structure of L-phenylalanine oxiase from Psuedomonas sp. P-501

Structural highlights

Function

Evolutionary Conservation

References

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