1pn0: Difference between revisions

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{{Seed}}
[[Image:1pn0.png|left|200px]]


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==Phenol hydroxylase from Trichosporon cutaneum==
The line below this paragraph, containing "STRUCTURE_1pn0", creates the "Structure Box" on the page.
<StructureSection load='1pn0' size='340' side='right'caption='[[1pn0]], [[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'>[[1pn0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cutaneotrichosporon_cutaneum Cutaneotrichosporon cutaneum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PN0 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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene></td></tr>
{{STRUCTURE_1pn0|  PDB=1pn0  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn0 OCA], [https://pdbe.org/1pn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1pn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHHY_CUTCT PHHY_CUTCT] Hydroxylates phenol to catechol (PubMed:1429434, PubMed:4146224, PubMed:3203745, PubMed:2022646, PubMed:7858421, PubMed:7851397, PubMed:11591156). Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cresols (PubMed:4146224, PubMed:17425111, PubMed:7851397).<ref>PMID:11591156</ref> <ref>PMID:1429434</ref> <ref>PMID:17425111</ref> <ref>PMID:2022646</ref> <ref>PMID:3203745</ref> <ref>PMID:4146224</ref> <ref>PMID:7851397</ref> <ref>PMID:7858421</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pn/1pn0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <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/main_output.php?pdb_ID=1pn0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure model of phenol hydroxylase has been corrected for 11 sequence errors and refined against new data to 1.7 A resolution. The higher resolution data together with careful exploitation of non-crystallographic symmetry restraints and the use of many small groups for refinement of anisotropic displacement parameters resulted in a large decrease in the crystallographic R factor. The final crystallographic free R factor is 18.0%, which should be compared with the values of 27.8% for the previously published model (PDB code 1foh). The rebuilding and re-refinement procedure is described. A comparison with the previously published model was performed and possible biochemical implications are discussed. No large differences suggesting gross errors in the earlier model were found. The actual differences between these two models give an indication of the level of ambiguity and inaccuracy that may be found in a well refined protein model at 2.4 A resolution.


===Phenol hydroxylase from Trichosporon cutaneum===
High-resolution structure of phenol hydroxylase and correction of sequence errors.,Enroth C Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:12925790<ref>PMID:12925790</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pn0" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12925790}}, adds the Publication Abstract to the page
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12925790 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_12925790}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Cutaneotrichosporon cutaneum]]
1PN0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trichosporon_cutaneum Trichosporon cutaneum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN0 OCA].
[[Category: Large Structures]]
 
[[Category: Enroth C]]
==Reference==
High-resolution structure of phenol hydroxylase and correction of sequence errors., Enroth C, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12925790 12925790]
[[Category: Phenol 2-monooxygenase]]
[[Category: Single protein]]
[[Category: Trichosporon cutaneum]]
[[Category: Enroth, C.]]
[[Category: Tls refinement]]
[[Category: Two dimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:48:47 2008''

Latest revision as of 12:45, 16 August 2023

Phenol hydroxylase from Trichosporon cutaneumPhenol hydroxylase from Trichosporon cutaneum

Structural highlights

1pn0 is a 4 chain structure with sequence from Cutaneotrichosporon cutaneum. 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:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHHY_CUTCT Hydroxylates phenol to catechol (PubMed:1429434, PubMed:4146224, PubMed:3203745, PubMed:2022646, PubMed:7858421, PubMed:7851397, PubMed:11591156). Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cresols (PubMed:4146224, PubMed:17425111, PubMed:7851397).[1] [2] [3] [4] [5] [6] [7] [8]

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 crystal structure model of phenol hydroxylase has been corrected for 11 sequence errors and refined against new data to 1.7 A resolution. The higher resolution data together with careful exploitation of non-crystallographic symmetry restraints and the use of many small groups for refinement of anisotropic displacement parameters resulted in a large decrease in the crystallographic R factor. The final crystallographic free R factor is 18.0%, which should be compared with the values of 27.8% for the previously published model (PDB code 1foh). The rebuilding and re-refinement procedure is described. A comparison with the previously published model was performed and possible biochemical implications are discussed. No large differences suggesting gross errors in the earlier model were found. The actual differences between these two models give an indication of the level of ambiguity and inaccuracy that may be found in a well refined protein model at 2.4 A resolution.

High-resolution structure of phenol hydroxylase and correction of sequence errors.,Enroth C Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:12925790[9]

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

See Also

References

  1. ↑ Xu D, Ballou DP, Massey V. Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met. Biochemistry. 2001 Oct 16;40(41):12369-78. PMID:11591156 doi:10.1021/bi010962y
  2. ↑ Kälin M, Neujahr HY, Weissmahr RN, Sejlitz T, Jöhl R, Fiechter A, Reiser J. Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli. J Bacteriol. 1992 Nov;174(22):7112-20. PMID:1429434 doi:10.1128/jb.174.22.7112-7120.1992
  3. ↑ Gerginova M, Manasiev J, Shivarova N, Alexieva Z. Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strain. Z Naturforsch C J Biosci. 2007 Jan-Feb;62(1-2):83-6. PMID:17425111 doi:10.1515/znc-2007-1-215
  4. ↑ Taylor MG, Massey V. Kinetic and isotopic studies of the oxidative half-reaction of phenol hydroxylase. J Biol Chem. 1991 May 5;266(13):8291-301 PMID:2022646
  5. ↑ Mörtberg M, Neujahr HY. Activation enthalpies and pH dependence of phenol hydroxylase from Trichosporon cutaneum, in vitro and in situ. FEBS Lett. 1988 Dec 19;242(1):75-8. PMID:3203745 doi:10.1016/0014-5793(88)80988-8
  6. ↑ Neujahr HY, Gaal A. Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum. Eur J Biochem. 1973 Jun;35(2):386-400. PMID:4146224 doi:10.1111/j.1432-1033.1973.tb02851.x
  7. ↑ Peelen S, Rietjens IM, Boersma MG, Vervoort J. Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics. Eur J Biochem. 1995 Jan 15;227(1-2):284-91. PMID:7851397 doi:10.1111/j.1432-1033.1995.tb20386.x
  8. ↑ Waters S, Neujahr HY. A fermentor culture for production of recombinant phenol hydroxylase. Protein Expr Purif. 1994 Dec;5(6):534-40. PMID:7858421 doi:10.1006/prep.1994.1073
  9. ↑ Enroth C. High-resolution structure of phenol hydroxylase and correction of sequence errors. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:12925790

1pn0, resolution 1.70Å

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