1irc

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[[Image:1irc.gif|left|200px]]
[[Image:1irc.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1irc |SIZE=350|CAPTION= <scene name='initialview01'>1irc</scene>, resolution 2.17&Aring;
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The line below this paragraph, containing "STRUCTURE_1irc", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=
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or leave the SCENE parameter empty for the default display.
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|GENE= SPERM WHALE MYOGLOBIN SYNTHETI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 Physeter catodon])
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-->
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|DOMAIN=
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{{STRUCTURE_1irc| PDB=1irc | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1irc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irc OCA], [http://www.ebi.ac.uk/pdbsum/1irc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1irc RCSB]</span>
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}}
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'''CYSTEINE RICH INTESTINAL PROTEIN'''
'''CYSTEINE RICH INTESTINAL PROTEIN'''
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[[Category: Barrick, D E.]]
[[Category: Barrick, D E.]]
[[Category: Feese, M.]]
[[Category: Feese, M.]]
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[[Category: heme]]
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[[Category: Heme]]
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[[Category: oxygen storage]]
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[[Category: Oxygen storage]]
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[[Category: respiratory protein]]
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[[Category: Respiratory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:19:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:33 2008''
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Revision as of 17:19, 2 May 2008

Image:1irc.gif

Template:STRUCTURE 1irc

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. 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 Fri May 2 20:19:11 2008

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