1s8c
From Proteopedia
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|PDB= 1s8c |SIZE=350|CAPTION= <scene name='initialview01'>1s8c</scene>, resolution 2.19Å | |PDB= 1s8c |SIZE=350|CAPTION= <scene name='initialview01'>1s8c</scene>, resolution 2.19Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BLA:BILIVERDINE IX ALPHA'>BLA</scene> | + | |LIGAND= <scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene> |
| - | |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] | + | |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> |
|GENE= HMOX1, HO1, HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= HMOX1, HO1, HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Epiphyseal dysplasia, multiple, 5 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602109 602109]], Heme oxygenase-1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141250 141250]], Osteoarthritis, hand, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602109 602109]], Spondyloepimetaphyseal dysplasia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602109 602109]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Montellano, P R.Ortiz de.]] | [[Category: Montellano, P R.Ortiz de.]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
| - | [[Category: BLA]] | ||
[[Category: heme degradation]] | [[Category: heme degradation]] | ||
[[Category: heme oxygenase-1]] | [[Category: heme oxygenase-1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:38:49 2008'' |
Revision as of 20:38, 30 March 2008
| |||||||
| , resolution 2.19Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | HMOX1, HO1, HO (Homo sapiens) | ||||||
| Activity: | Heme oxygenase, with EC number 1.14.99.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:38:49 2008
