1ac8: Difference between revisions

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-[[Image:1ac8.gif|left|200px]]
- {{Structure
+==VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)==
-|PDB= 1ac8 |SIZE=350|CAPTION= <scene name='initialview01'>1ac8</scene>, resolution 2.1&Aring;
+<StructureSection load='1ac8' size='340' side='right'caption='[[1ac8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AVE:Removal+Of+TRP+191+Forms+An+Internal+Cavity+Below+The+He+...'>AVE</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=TMZ:3,4,5-TRIMETHYL-1,3-THIAZOLE'>TMZ</scene>
+<table><tr><td colspan='2'>[[1ac8]] 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=1AC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AC8 FirstGlance]. <br>
-|ACTIVITY= [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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-|GENE= CCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TMZ:3,4,5-TRIMETHYL-1,3-THIAZOLE'>TMZ</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=1ac8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac8 OCA], [https://pdbe.org/1ac8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ac8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ac8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ac8 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/ac/1ac8_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=1ac8 ConSurf].
+<div style="clear:both"></div>
-'''VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)'''
+==See Also==
+*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-AC8 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=1AC8 OCA].
-==Reference==
-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]
-[[Category: Cytochrome-c peroxidase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Bunte SW]]
-[[Category: Bunte, S W.]]
+[[Category: Goodin DB]]
-[[Category: Goodin, D B.]]
+[[Category: Jensen GM]]
-[[Category: Jensen, G M.]]
+[[Category: Mcree DE]]
-[[Category: Mcree, D E.]]
+[[Category: Musah RA]]
-[[Category: Musah, R A.]]
+[[Category: Rosenfeld R]]
-[[Category: Rosenfeld, R.]]
-[[Category: HEM]]
-[[Category: TMZ]]
-[[Category: oxidoreductase]]
-[[Category: peroxidase]]
-[[Category: transit peptide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:55:37 2008''