2e7e

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[[Image:2e7e.jpg|left|200px]]
[[Image:2e7e.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2e7e |SIZE=350|CAPTION= <scene name='initialview01'>2e7e</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_2e7e", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2e7e| PDB=2e7e | SCENE= }}
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|RELATEDENTRY=[[1ix3|1IX3]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e7e OCA], [http://www.ebi.ac.uk/pdbsum/2e7e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e7e RCSB]</span>
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}}
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'''Bent-binding of cyanide to the heme iron in rat heme oxygenase-1'''
'''Bent-binding of cyanide to the heme iron in rat heme oxygenase-1'''
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[[Category: Fukuyama, K.]]
[[Category: Fukuyama, K.]]
[[Category: Sugishima, M.]]
[[Category: Sugishima, M.]]
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[[Category: binding geometry]]
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[[Category: Binding geometry]]
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[[Category: heme]]
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[[Category: Heme]]
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[[Category: ligand]]
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[[Category: Ligand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:04:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:44:51 2008''
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Revision as of 23:04, 3 May 2008

Template:STRUCTURE 2e7e

Bent-binding of cyanide to the heme iron in rat heme oxygenase-1


Overview

Cyanide is a well known potent inhibitor of haem proteins, including haem oxygenase (HO). Generally, cyanide coordinates to the ferric haem iron with a linear binding geometry; the Fe-C-N angle ranges from 160 to 180 degrees . The Fe-C-N angle observed in the crystal structure of haem-HO bound to cyanide prepared at alkaline pH was 166 degrees . Here, it is reported that cyanide can bind to the haem iron in HO in a bent mode when the ternary complex is prepared at neutral pH; a crystal structure showed that the Fe-C-N angle was bent by 47 degrees . Unlike the ternary complex prepared at alkaline pH, in which the haem group, including the proximal ligand and the distal helix, was displaced upon cyanide binding, the positions of the haem group and the distal helix in the complex prepared at neutral pH were nearly identical to those in haem-HO. Cyanide that was bound to haem-HO with a bent geometry was readily photodissociated, whereas that bound with a linear geometry was not photodissociated. Thus, alternative cyanide-binding modes with linear and bent geometries exist in the crystalline state of haem-HO.

About this Structure

2E7E is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Alternative cyanide-binding modes to the haem iron in haem oxygenase., Sugishima M, Oda K, Ogura T, Sakamoto H, Noguchi M, Fukuyama K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):471-4. Epub 2007 May 31. PMID:17554165 Page seeded by OCA on Sun May 4 02:04:22 2008

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