1ccg: Difference between revisions
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|PDB= 1ccg |SIZE=350|CAPTION= <scene name='initialview01'>1ccg</scene>, resolution 2.1Å | |PDB= 1ccg |SIZE=350|CAPTION= <scene name='initialview01'>1ccg</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene> | ||
|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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ccg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccg OCA], [http://www.ebi.ac.uk/pdbsum/1ccg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ccg RCSB]</span> | |||
}} | }} | ||
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[[Category: Mcree, D E.]] | [[Category: Mcree, D E.]] | ||
[[Category: Siegel, H A.]] | [[Category: Siegel, H A.]] | ||
[[Category: oxidoreductase(h2o2(a))]] | [[Category: oxidoreductase(h2o2(a))]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:05 2008'' | ||
Revision as of 19:19, 30 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND
OverviewOverview
The crystal structure of the His-175-->Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo heme protein. This protein retains some residual activity, which can be stimulated or inhibited by addition of exogenous ligands. Structural analysis confirms the binding of imidazole to the heme at the position of the wild-type histidine ligand. This imidazole complex reacts readily with hydrogen peroxide to produce a radical species with novel properties. However, reactivation in this complex is incomplete (approximately 5%), which, in view of the very similar structures of the wild-type and the H175G/imidazole forms, implies a critical role for tethering of the axial ligand in catalysis. This study demonstrates the feasibility of constructing heme enzymes with no covalent link to the protein and with unnatural ligand replacements. Such enzymes may prove useful in studies of electron transfer mechanisms and in the engineering of novel heme-based catalysts.
About this StructureAbout this Structure
1CCG is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Construction of a bisaquo heme enzyme and binding by exogenous ligands., McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB, Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:7809133
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