1iw0: Difference between revisions

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[[Image:1iw0.jpg|left|200px]]<br /><applet load="1iw0" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1iw0.jpg|left|200px]]
caption="1iw0, resolution 1.40&Aring;" />
 
'''Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferric state'''<br />
{{Structure
|PDB= 1iw0 |SIZE=350|CAPTION= <scene name='initialview01'>1iw0</scene>, resolution 1.40&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</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=
}}
 
'''Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferric state'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1IW0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] with <scene name='pdbligand=SUC:'>SUC</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1IW0 OCA].  
1IW0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IW0 OCA].  


==Reference==
==Reference==
The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae., Hirotsu S, Chu GC, Unno M, Lee DS, Yoshida T, Park SY, Shiro Y, Ikeda-Saito M, J Biol Chem. 2004 Mar 19;279(12):11937-47. Epub 2003 Nov 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14645223 14645223]
The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae., Hirotsu S, Chu GC, Unno M, Lee DS, Yoshida T, Park SY, Shiro Y, Ikeda-Saito M, J Biol Chem. 2004 Mar 19;279(12):11937-47. Epub 2003 Nov 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14645223 14645223]
[[Category: Corynebacterium diphtheriae]]
[[Category: Corynebacterium diphtheriae]]
[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
[[Category: structural genomics]]
[[Category: structural genomic]]


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Revision as of 12:55, 20 March 2008

File:1iw0.jpg


PDB ID 1iw0

Drag the structure with the mouse to rotate
, resolution 1.40Å
Ligands: , and
Activity: Heme oxygenase, with EC number 1.14.99.3
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferric state


OverviewOverview

Crystal structures of the ferric and ferrous heme complexes of HmuO, a 24-kDa heme oxygenase of Corynebacterium diphtheriae, have been refined to 1.4 and 1.5 A resolution, respectively. The HmuO structures show that the heme group is closely sandwiched between the proximal and distal helices. The imidazole group of His-20 is the proximal heme ligand, which closely eclipses the beta- and delta-meso axis of the porphyrin ring. A long range hydrogen bonding network is present, connecting the iron-bound water ligand to the solvent water molecule. This enables proton transfer from the solvent to the catalytic site, where the oxygen activation occurs. In comparison to the ferric complex, the proximal and distal helices move closer to the heme plane in the ferrous complex. Together with the kinked distal helix, this movement leaves only the alpha-meso carbon atom accessible to the iron-bound dioxygen. The heme pocket architecture is responsible for stabilization of the ferric hydroperoxo-active intermediate by preventing premature heterolytic O-O bond cleavage. This allows the enzyme to oxygenate selectively at the alpha-meso carbon in HmuO catalysis.

About this StructureAbout this Structure

1IW0 is a Single protein structure of sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae., Hirotsu S, Chu GC, Unno M, Lee DS, Yoshida T, Park SY, Shiro Y, Ikeda-Saito M, J Biol Chem. 2004 Mar 19;279(12):11937-47. Epub 2003 Nov 26. PMID:14645223

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