1xk0: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1xk0.gif|left|200px]] | [[Image:1xk0.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1xk0", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1xk0| PDB=1xk0 | SCENE= }} | |||
}} | |||
'''Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1''' | '''Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1''' | ||
Line 30: | Line 27: | ||
[[Category: Montellano, P R.Ortiz de.]] | [[Category: Montellano, P R.Ortiz de.]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
[[Category: | [[Category: Heme]] | ||
[[Category: | [[Category: Heme degredation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:07:43 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 15:07, 3 May 2008
Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
OverviewOverview
Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis. Earlier mutagenesis work on human HO-1 showed that replacement of either Gly139 or Gly143 suppresses heme oxygenase activity and, in the case of the Gly139 mutants, increases peroxidase activity (Liu et al. in J. Biol. Chem. 275:34501, 2000). To further investigate the role of the conserved distal helix glycines, we have determined the crystal structures of the human HO-1 G139A mutant, the G139A mutant in a complex with NO, and the G143H mutant at 1.88, 2.18 and 2.08 A, respectively. The results confirm that fine tuning of the previously noted active-site hydrogen-bonding network is critical in determining whether heme oxygenase or peroxidase activity is observed.
About this StructureAbout this Structure
1XK0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity., Lad L, Koshkin A, de Montellano PR, Poulos TL, J Biol Inorg Chem. 2005 Mar;10(2):138-46. Epub 2005 Feb 3. PMID:15690204 Page seeded by OCA on Sat May 3 15:07:43 2008