1iw0: Difference between revisions

Line 1:

[[Image:1iw0.jpg|left|200px]]<br /><applet load="1iw0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1iw0.jpg|left|200px]]<br /><applet load="1iw0" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1iw0, resolution 1.40Å" />

'''Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferric state'''<br />

==Overview==

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.

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 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 SUC, SO4 and HEM 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1IW0 OCA].

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].

==Reference==

Line 14:

[[Category: Heme oxygenase]]

[[Category: Single protein]]

[[Category: Chu, G.C.]]

[[Category: Chu, G C.]]

[[Category: Hirotsu, S.]]

[[Category: Ikeda-Saito, M.]]

[[Category: Lee, D.S.]]

[[Category: Lee, D S.]]

[[Category: Park, S.Y.]]

[[Category: Park, S Y.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Shiro, Y.]]

[[Category: Unno, M.]]

Line 31:

[[Category: structural genomics]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:42:~~54 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:13 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1iw0.jpg|left|200px]]<br /><applet load="1iw0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1iw0.jpg|left|200px]]<br /><applet load="1iw0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1iw0, resolution 1.40&Aring;" />
 '''Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferric state'''<br />
 ==Overview==
-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.
+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 Structure==
-IW0 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 SUC, SO4 and HEM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IW0 OCA].
+IW0 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].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Heme oxygenase]]
 [[Category: Single protein]]
-[[Category: Chu, G.C.]]
+[[Category: Chu, G C.]]
 [[Category: Hirotsu, S.]]
 [[Category: Ikeda-Saito, M.]]
-[[Category: Lee, D.S.]]
+[[Category: Lee, D S.]]
-[[Category: Park, S.Y.]]
+[[Category: Park, S Y.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Shiro, Y.]]
 [[Category: Unno, M.]]
@@ Line 31: / Line 31: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:42:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:13 2008''