1ryc: Difference between revisions

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New page: left|200px<br /><applet load="1ryc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryc, resolution 1.8Å" /> '''CYTOCHROME C PEROXIDA...
 
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[[Image:1ryc.jpg|left|200px]]<br /><applet load="1ryc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ryc, resolution 1.8&Aring;" />
'''CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE'''<br />


==Overview==
==CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE==
Conformational changes that gate the access of substrates or ligands to an, active site are important features of enzyme function. In this report, we, describe an unusual example of a structural rearrangement near a buried, artificial cavity in cytochrome c peroxidase that occurs on binding, protonated benzimidazole. A hinged main-chain rotation at two residues, (Pro 190 and Asn 195) results in a surface loop rearrangement that opens a, large solvent-accessible channel for the entry of ligands to an otherwise, inaccessible binding site. The trapping of this alternate conformational, state provides a unique view of the extent to which protein dynamics can, allow small molecule penetration into buried protein cavities.
<StructureSection load='1ryc' size='340' side='right'caption='[[1ryc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ryc]] 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=1RYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RYC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BZI:BENZIMIDAZOLE'>BZI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1ryc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ryc OCA], [https://pdbe.org/1ryc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ryc RCSB], [https://www.ebi.ac.uk/pdbsum/1ryc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ryc 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/ry/1ryc_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=1ryc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1RYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with HEM and BZI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RYC OCA].
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity., Fitzgerald MM, Musah RA, McRee DE, Goodin DB, Nat Struct Biol. 1996 Jul;3(7):626-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8673607 8673607]
[[Category: Large Structures]]
[[Category: Cytochrome-c peroxidase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Fitzgerald MM]]
[[Category: Fitzgerald, M.M.]]
[[Category: Goodin DB]]
[[Category: Goodin, D.B.]]
[[Category: Mcree DE]]
[[Category: Mcree, D.E.]]
[[Category: Musah R]]
[[Category: Musah, R.]]
[[Category: BZI]]
[[Category: HEM]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:57:25 2007''

Latest revision as of 11:26, 14 February 2024

CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAECYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE

Structural highlights

1ryc 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 1.8Å
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

1ryc, resolution 1.80Å

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