1cf9

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[[Image:1cf9.gif|left|200px]]
[[Image:1cf9.gif|left|200px]]
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{{Structure
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|PDB= 1cf9 |SIZE=350|CAPTION= <scene name='initialview01'>1cf9</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1cf9", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span>
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{{STRUCTURE_1cf9| PDB=1cf9 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf9 OCA], [http://www.ebi.ac.uk/pdbsum/1cf9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cf9 RCSB]</span>
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'''STRUCTURE OF THE MUTANT VAL169CYS OF CATALASE HPII FROM ESCHERICHIA COLI'''
'''STRUCTURE OF THE MUTANT VAL169CYS OF CATALASE HPII FROM ESCHERICHIA COLI'''
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[[Category: Loewen, P C.]]
[[Category: Loewen, P C.]]
[[Category: Mate, M J.]]
[[Category: Mate, M J.]]
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[[Category: covalent modification]]
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[[Category: Covalent modification]]
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[[Category: hydrogen peroxide]]
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[[Category: Hydrogen peroxide]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:40:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:29 2008''
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Revision as of 09:40, 2 May 2008

Image:1cf9.gif

Template:STRUCTURE 1cf9

STRUCTURE OF THE MUTANT VAL169CYS OF CATALASE HPII FROM ESCHERICHIA COLI


Overview

The three-dimensional structures of two HPII variants, V169C and H392Q, have been determined at resolutions of 1.8 and 2.1 A, respectively. The V169C variant contains a new type of covalent bond between the sulfur atom of Cys(169) and a carbon atom on the imidazole ring of the essential His(128). This variant enzyme has only residual catalytic activity and contains heme b. The chain of water molecules visible in the main channel may reflect the organization of the hydrogen peroxide substrates in the active enzyme. Two alternative mechanisms, involving either compound I or free radical intermediates, are presented to explain the formation of the Cys-His covalent bond. The H392Q and H392E variants exhibit 75 and 25% of native catalytic activity, respectively. The Gln(392) variant contains only heme b, whereas the Glu(392) variant contains a mixture of heme b and cis and trans isomers of heme d, suggesting of a role for this residue in heme conversion. Replacement of either Gln(419) and Ser(414), both of which interact with the heme, affected the cis:trans ratio of spirolactone heme d. Implications for the heme oxidation mechanism and the His-Tyr bond formation in HPII are considered.

About this Structure

1CF9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli., Mate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I, J Biol Chem. 1999 Sep 24;274(39):27717-25. PMID:10488114 Page seeded by OCA on Fri May 2 12:40:12 2008

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