This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1s8c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1s8c.jpg|left|200px]]<br /><applet load="1s8c" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1s8c.jpg|left|200px]]
-
caption="1s8c, resolution 2.19&Aring;" />
+
 
-
'''Crystal structure of human heme oxygenase in a complex with biliverdine'''<br />
+
{{Structure
 +
|PDB= 1s8c |SIZE=350|CAPTION= <scene name='initialview01'>1s8c</scene>, resolution 2.19&Aring;
 +
|SITE=
 +
|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]
 +
|GENE= HMOX1, HO1, HO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''Crystal structure of human heme oxygenase in a complex with biliverdine'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
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].
+
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==
-
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]
+
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]]
Line 27: Line 36:
[[Category: heme oxygenase-1]]
[[Category: heme oxygenase-1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:00 2008''
+
''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

Page seeded by OCA on Thu Mar 20 14:01:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools