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[[Image:1cci.gif|left|200px]]
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{{STRUCTURE_1cci|  PDB=1cci  |  SCENE=  }}
'''HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP'''


==HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP==
<StructureSection load='1cci' size='340' side='right'caption='[[1cci]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cci]] 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=1CCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCI 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMI:2,3-DIMETHYLIMIDAZOLIUM+ION'>DMI</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=1cci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cci OCA], [https://pdbe.org/1cci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cci RCSB], [https://www.ebi.ac.uk/pdbsum/1cci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cci 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/cc/1cci_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1cci ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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:8673607<ref>PMID:8673607</ref>
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.


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


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/8673607 8673607]
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
[[Category: Cytochrome-c peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Cao Y]]
[[Category: Cao, Y.]]
[[Category: Goodin DB]]
[[Category: Goodin, D B.]]
[[Category: Mcree DE]]
[[Category: Mcree, D E.]]
[[Category: Musah RA]]
[[Category: Musah, R A.]]
[[Category: Wilcox SK]]
[[Category: Wilcox, S K.]]
[[Category: Heme]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
[[Category: Polymorphism]]
[[Category: Transit peptide]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:34:58 2008''

Latest revision as of 05:33, 13 August 2026

HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP

1cci, resolution 2.40Å

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