1irc
From Proteopedia
(New page: 200px<br /><applet load="1irc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1irc, resolution 2.17Å" /> '''CYSTEINE RICH INTEST...) |
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| - | [[Image:1irc.gif|left|200px]]<br /><applet load="1irc" size=" | + | [[Image:1irc.gif|left|200px]]<br /><applet load="1irc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1irc, resolution 2.17Å" /> | caption="1irc, resolution 2.17Å" /> | ||
'''CYSTEINE RICH INTESTINAL PROTEIN'''<br /> | '''CYSTEINE RICH INTESTINAL PROTEIN'''<br /> | ||
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| + | ==Overview== | ||
| + | The proximal bond between the iron atom of the heme group and the N epsilon of histidine F8 in myoglobin (Mb) and hemoglobin (Hb) is presumed to be an important determinant of heme binding, protein structure, and oxygen binding. Here a system is described in which the proximal ligand is provided intermolecularly by the histidine side chain mimic imidazole. The proximal ligand of sperm whale Mb is replaced with glycine (H93G) using site-directed mutagenesis. The addition of imidazole to Escherichia coli expressing this gene reconstitutes myoglobin function. H93G Mb purified in the presence of imidazole is spectroscopically similar to wild-type Mb in combination with a wide variety of distal ligands. The crystal structure of H93G Mb, determined in the presence of imidazole, reveals that an imidazole molecule is bonded to the heme iron on the proximal side, substituting in trans for the side-chain function of the proximal histidine of wild-type Mb. Although H93G Mb is similar in spectroscopic and gross structural detail to wild-type Mb, subtle differences exist in the orientation of imidazole with respect to the heme group. trans-Complementation of proximal ligand function will allow the proximal bond in hemoproteins to be chemically substituted beyond the limits of the genetic code. | ||
==About this Structure== | ==About this Structure== | ||
| - | 1IRC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with HEM and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1IRC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRC OCA]. |
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| + | ==Reference== | ||
| + | Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly., Barrick D, Biochemistry. 1994 May 31;33(21):6546-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8204590 8204590] | ||
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barrick, D | + | [[Category: Barrick, D E.]] |
[[Category: Feese, M.]] | [[Category: Feese, M.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:46 2008'' |
Revision as of 11:14, 21 February 2008
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CYSTEINE RICH INTESTINAL PROTEIN
Overview
The proximal bond between the iron atom of the heme group and the N epsilon of histidine F8 in myoglobin (Mb) and hemoglobin (Hb) is presumed to be an important determinant of heme binding, protein structure, and oxygen binding. Here a system is described in which the proximal ligand is provided intermolecularly by the histidine side chain mimic imidazole. The proximal ligand of sperm whale Mb is replaced with glycine (H93G) using site-directed mutagenesis. The addition of imidazole to Escherichia coli expressing this gene reconstitutes myoglobin function. H93G Mb purified in the presence of imidazole is spectroscopically similar to wild-type Mb in combination with a wide variety of distal ligands. The crystal structure of H93G Mb, determined in the presence of imidazole, reveals that an imidazole molecule is bonded to the heme iron on the proximal side, substituting in trans for the side-chain function of the proximal histidine of wild-type Mb. Although H93G Mb is similar in spectroscopic and gross structural detail to wild-type Mb, subtle differences exist in the orientation of imidazole with respect to the heme group. trans-Complementation of proximal ligand function will allow the proximal bond in hemoproteins to be chemically substituted beyond the limits of the genetic code.
About this Structure
1IRC is a Single protein structure of sequence from Physeter catodon with and as ligands. Full crystallographic information is available from OCA.
Reference
Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly., Barrick D, Biochemistry. 1994 May 31;33(21):6546-54. PMID:8204590
Page seeded by OCA on Thu Feb 21 13:14:46 2008
