1aes: Difference between revisions
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<StructureSection load='1aes' size='340' side='right'caption='[[1aes]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1aes' size='340' side='right'caption='[[1aes]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1aes]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1aes]] 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=1AES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AES FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <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=IMD:IMIDAZOLE'>IMD</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=1aes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aes OCA], [https://pdbe.org/1aes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aes RCSB], [https://www.ebi.ac.uk/pdbsum/1aes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aes ProSAT]</span></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=1aes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aes OCA], [https://pdbe.org/1aes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aes RCSB], [https://www.ebi.ac.uk/pdbsum/1aes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aes ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Fitzgerald MM]] | ||
[[Category: | [[Category: Goodin DB]] | ||
[[Category: | [[Category: Jensen GM]] | ||
[[Category: | [[Category: Mcree DE]] | ||
[[Category: | [[Category: Musah RA]] | ||
Latest revision as of 13:51, 2 August 2023
SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE (IMIDAZOLE)SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE (IMIDAZOLE)
Structural highlights
FunctionCCPR_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. Publication Abstract from PubMedConformational 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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