1mdv
From Proteopedia
(New page: 200px<br /><applet load="1mdv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mdv, resolution 2.3Å" /> '''KEY ROLE OF PHENYLALA...) |
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| - | [[Image:1mdv.gif|left|200px]]<br /><applet load="1mdv" size=" | + | [[Image:1mdv.gif|left|200px]]<br /><applet load="1mdv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mdv, resolution 2.3Å" /> | caption="1mdv, resolution 2.3Å" /> | ||
'''KEY ROLE OF PHENYLALANINE 20 IN CYTOCHROME C3: STRUCTURE, STABILITY AND FUNCTION STUDIES'''<br /> | '''KEY ROLE OF PHENYLALANINE 20 IN CYTOCHROME C3: STRUCTURE, STABILITY AND FUNCTION STUDIES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Aromatic residues in c-type cytochromes might have an important function | + | Aromatic residues in c-type cytochromes might have an important function in the folding and/or electron transferring properties of the molecule. In the tetraheme cytochrome c3 (Mr 13 000) from Desulfovibrio vulgaris Hildenborough, Phe20, is located between heme 1 and heme 3 with its aromatic ring close and almost parallel to the ring plane of heme 1. We replaced this residue by a nonaromatic hydrophobe residue, leucine, and analyzed the effects in terms of functional, structural, and physicochemical properties. While the F20L replacement did not have any strong effects on the heme region stability, a decrease of the thermostability of the whole molecule was observed. In the same way, the four macroscopic redox potentials were affected by the mutation as well as the flexibility of the surface loop around heme 4. The F20L replacement itself and/or this structural modification might be responsible for the loss of the intermolecular cooperativity between F20L cytochrome c3 molecules. |
==About this Structure== | ==About this Structure== | ||
| - | 1MDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Czjzek, M.]] | [[Category: Czjzek, M.]] | ||
[[Category: Dolla, A.]] | [[Category: Dolla, A.]] | ||
| - | [[Category: Guidici-Orticoni, M | + | [[Category: Guidici-Orticoni, M T.]] |
[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
[[Category: Lobachov, V.]] | [[Category: Lobachov, V.]] | ||
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[[Category: mutant cytochrome c3]] | [[Category: mutant cytochrome c3]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:14 2008'' |
Revision as of 11:54, 21 February 2008
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KEY ROLE OF PHENYLALANINE 20 IN CYTOCHROME C3: STRUCTURE, STABILITY AND FUNCTION STUDIES
Overview
Aromatic residues in c-type cytochromes might have an important function in the folding and/or electron transferring properties of the molecule. In the tetraheme cytochrome c3 (Mr 13 000) from Desulfovibrio vulgaris Hildenborough, Phe20, is located between heme 1 and heme 3 with its aromatic ring close and almost parallel to the ring plane of heme 1. We replaced this residue by a nonaromatic hydrophobe residue, leucine, and analyzed the effects in terms of functional, structural, and physicochemical properties. While the F20L replacement did not have any strong effects on the heme region stability, a decrease of the thermostability of the whole molecule was observed. In the same way, the four macroscopic redox potentials were affected by the mutation as well as the flexibility of the surface loop around heme 4. The F20L replacement itself and/or this structural modification might be responsible for the loss of the intermolecular cooperativity between F20L cytochrome c3 molecules.
About this Structure
1MDV is a Single protein structure of sequence from Desulfovibrio vulgaris with as ligand. Full crystallographic information is available from OCA.
Reference
Key role of phenylalanine 20 in cytochrome c3: structure, stability, and function studies., Dolla A, Arnoux P, Protasevich I, Lobachov V, Brugna M, Giudici-Orticoni MT, Haser R, Czjzek M, Makarov A, Bruschi M, Biochemistry. 1999 Jan 5;38(1):33-41. PMID:9890880
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