1ml2: Difference between revisions

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[[Image:1ml2.gif|left|200px]]


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==Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)==
The line below this paragraph, containing "STRUCTURE_1ml2", creates the "Structure Box" on the page.
<StructureSection load='1ml2' size='340' side='right'caption='[[1ml2]], [[Resolution|resolution]] 1.65&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'>[[1ml2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ML2 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]] 1.65&#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=ZEM:20-OXO-PROTOPORPHYRIN+IX+CONTAINING+ZN(II)'>ZEM</scene></td></tr>
{{STRUCTURE_1ml2| PDB=1ml2 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ml2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ml2 OCA], [https://pdbe.org/1ml2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ml2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ml2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ml2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
== 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/ml/1ml2_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=1ml2 ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)'''
==See Also==
 
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structure of a cytochrome c peroxidase mutant where the distal catalytic His52 is converted to Tyr reveals that the tyrosine side-chain forms a covalent bond with the indole ring nitrogen atom of Trp51. We hypothesize that this novel bond results from peroxide activation by the heme iron followed by oxidation of Trp51 and Tyr52. This hypothesis has been tested by incorporation of a redox-inactive Zn-protoporphyrin into the protein, and the resulting crystal structure shows the absence of a Trp51-Tyr52 cross-link. Instead, the Tyr52 side-chain orients away from the heme active-site pocket, which requires a substantial rearrangement of residues 72-80 and 134-144. Additional experiments where heme-containing crystals of the mutant were treated with peroxide support our hypothesis that this novel Trp-Tyr cross-link is a peroxide-dependent process mediated by the heme iron.
[[Category: Large Structures]]
 
==About this Structure==
1ML2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML2 OCA].
 
==Reference==
A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase., Bhaskar B, Immoos CE, Shimizu H, Sulc F, Farmer PJ, Poulos TL, J Mol Biol. 2003 Apr 18;328(1):157-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12684005 12684005]
[[Category: Cytochrome-c peroxidase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Bhaskar B]]
[[Category: Bhaskar, B.]]
[[Category: Farmer PJ]]
[[Category: Farmer, P J.]]
[[Category: Immoos CE]]
[[Category: Immoos, C E.]]
[[Category: Poulos TL]]
[[Category: Poulos, T L.]]
[[Category: Shimizu H]]
[[Category: Shimizu, H.]]
[[Category: Cytochrome c peroxidase]]
[[Category: Oxygen radical]]
[[Category: Trp cation radical]]
[[Category: Trp-tyr covalent cross-link]]
[[Category: Zn-protoporphyrin ix]]
[[Category: Znccp]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:21:04 2008''

Latest revision as of 10:45, 14 February 2024

Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)

Structural highlights

1ml2 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Evolutionary Conservation

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

See Also

1ml2, resolution 1.65Å

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