1dve: Difference between revisions
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==CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME== | ==CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME== | ||
<StructureSection load='1dve' size='340' side='right' caption='[[1dve]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1dve' size='340' side='right'caption='[[1dve]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dve]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DVE FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dve]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DVE FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1dve" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1dve" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Buffalo rat]] | [[Category: Buffalo rat]] | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Fukuyama, K]] | [[Category: Fukuyama, K]] | ||
[[Category: Kakuta, Y]] | [[Category: Kakuta, Y]] | ||
Revision as of 16:38, 16 October 2019
CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEMECRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME
Structural highlights
Function[HMOX1_RAT] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHeme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of heme metabolism utilizing O(2) and NADPH. We determined the crystal structures of rat heme oxygenase-1 (HO-1)-heme and selenomethionyl HO-1-heme complexes. Heme is sandwiched between two helices with the delta-meso edge of the heme being exposed to the surface. Gly143N forms a hydrogen bond to the distal ligand of heme, OH(-). The distance between Gly143N and the ligand is shorter than that in the human HO-1-heme complex. This difference may be related to a pH-dependent change of the distal ligand of heme. Flexibility of the distal helix may control the stability of the coordination of the distal ligand to heme iron. The possible role of Gly143 in the heme oxygenase reaction is discussed. Crystal structure of rat heme oxygenase-1 in complex with heme.,Sugishima M, Omata Y, Kakuta Y, Sakamoto H, Noguchi M, Fukuyama K FEBS Lett. 2000 Apr 7;471(1):61-6. PMID:10760513[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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