1s8c

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[[Image:1s8c.jpg|left|200px]]<br /><applet load="1s8c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s8c.jpg|left|200px]]
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caption="1s8c, resolution 2.19&Aring;" />
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'''Crystal structure of human heme oxygenase in a complex with biliverdine'''<br />
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{{Structure
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|PDB= 1s8c |SIZE=350|CAPTION= <scene name='initialview01'>1s8c</scene>, resolution 2.19&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BLA:BILIVERDINE IX ALPHA'>BLA</scene>
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|ACTIVITY= [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]
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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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}}
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'''Crystal structure of human heme oxygenase in a complex with biliverdine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1S8C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=BLA:'>BLA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S8C OCA].
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1S8C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S8C OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15049686 15049686]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15049686 15049686]
[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: heme oxygenase-1]]
[[Category: heme oxygenase-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:01:49 2008''

Revision as of 12:01, 20 March 2008


PDB ID 1s8c

Drag the structure with the mouse to rotate
, resolution 2.19Å
Ligands:
Gene: HMOX1, HO1, HO (Homo sapiens)
Activity: Heme oxygenase, with EC number 1.14.99.3
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human heme oxygenase in a complex with biliverdine


Contents

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.

Disease

Known diseases associated with this structure: Epiphyseal dysplasia, multiple, 5 OMIM:[602109], Heme oxygenase-1 deficiency OMIM:[141250], Osteoarthritis, hand, susceptibility to OMIM:[602109], Spondyloepimetaphyseal dysplasia OMIM:[602109]

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

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