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1s8c

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[[Image:1s8c.jpg|left|200px]]
[[Image:1s8c.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1s8c |SIZE=350|CAPTION= <scene name='initialview01'>1s8c</scene>, resolution 2.19&Aring;
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The line below this paragraph, containing "STRUCTURE_1s8c", 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=BLA:BILIVERDINE+IX+ALPHA'>BLA</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/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= HMOX1, HO1, HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1s8c| PDB=1s8c | 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=1s8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s8c OCA], [http://www.ebi.ac.uk/pdbsum/1s8c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s8c RCSB]</span>
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'''Crystal structure of human heme oxygenase in a complex with biliverdine'''
'''Crystal structure of human heme oxygenase in a complex with biliverdine'''
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[[Category: Montellano, P R.Ortiz de.]]
[[Category: Montellano, P R.Ortiz de.]]
[[Category: Poulos, T L.]]
[[Category: Poulos, T L.]]
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[[Category: heme degradation]]
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[[Category: Heme degradation]]
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[[Category: heme oxygenase-1]]
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[[Category: Heme oxygenase-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:25:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:38:49 2008''
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Revision as of 05:25, 3 May 2008

Template:STRUCTURE 1s8c

Crystal structure of human heme oxygenase in a complex with biliverdine


Overview

Heme oxygenase oxidatively cleaves heme to biliverdin, leading to the release of iron and CO through a process in which the heme participates both as a cofactor and as a substrate. Here we report the crystal structure of the product, iron-free biliverdin, in a complex with human HO-1 at 2.19 A. Structural comparisons of the human biliverdin-HO-1 structure with its heme complex and the recently published rat HO-1 structure in a complex with the biliverdin-iron chelate [Sugishima, M., Sakamoto, H., Higashimoto, Y., Noguchi, M., and Fukuyama, K. (2003) J. Biol. Chem. 278, 32352-32358] show two major differences. First, in the absence of an Fe-His bond and solvent structure in the active site, the distal and proximal helices relax and adopt an "open" conformation which most likely encourages biliverdin release. Second, iron-free biliverdin occupies a different position and orientation relative to heme and the biliverdin-iron complex. Biliverdin adopts a more linear conformation and moves from the heme site to an internal cavity. These structural results provide insight into the rate-limiting step in HO-1 catalysis, which is product, biliverdin, release.

About this Structure

1S8C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human heme oxygenase-1 in a complex with biliverdin., Lad L, Friedman J, Li H, Bhaskar B, Ortiz de Montellano PR, Poulos TL, Biochemistry. 2004 Apr 6;43(13):3793-801. PMID:15049686 Page seeded by OCA on Sat May 3 08:25:25 2008

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