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1ac4

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(New page: 200px<br /> <applet load="1ac4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ac4, resolution 2.1&Aring;" /> '''VARIATION IN THE STR...)
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[[Image:1ac4.gif|left|200px]]<br />
 
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<applet load="1ac4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ac4, resolution 2.1&Aring;" />
 
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'''VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2,3,4-TRIMETHYL-1,3-THIAZOLE)'''<br />
 
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==Overview==
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==VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2,3,4-TRIMETHYL-1,3-THIAZOLE)==
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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.
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<StructureSection load='1ac4' size='340' side='right'caption='[[1ac4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ac4]] 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=1AC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AC4 FirstGlance]. <br>
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</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>
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<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=TMT:2,3,4-TRIMETHYL-1,3-THIAZOLE'>TMT</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ac4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac4 OCA], [https://pdbe.org/1ac4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ac4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ac4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ac4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/1ac4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ac4 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AC4 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 TMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1AC4 OCA]].
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Bunte SW]]
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[[Category: Bunte, S.W.]]
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[[Category: Goodin DB]]
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[[Category: Goodin, D.B.]]
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[[Category: Jensen GM]]
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[[Category: Jensen, G.M.]]
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[[Category: Mcree DE]]
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[[Category: Mcree, D.E.]]
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[[Category: Musah RA]]
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[[Category: Musah, R.A.]]
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[[Category: Rosenfeld R]]
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[[Category: Rosenfeld, R.]]
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[[Category: HEM]]
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[[Category: TMT]]
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[[Category: oxidoreductase]]
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[[Category: peroxidase]]
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[[Category: transit peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:16:44 2007''
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Current revision

VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2,3,4-TRIMETHYL-1,3-THIAZOLE)

PDB ID 1ac4

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