1c1h: Difference between revisions

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[[Image:1c1h.jpg|left|200px]]<br /><applet load="1c1h" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1c1h.jpg|left|200px]]<br /><applet load="1c1h" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1c1h, resolution 1.90Å" />

'''CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN'''<br />

==Overview==

Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at, the terminal step of heme biosynthesis, was co-crystallized with an isomer, mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray, structure revealed the active site of the enzyme, to which only one of the, isomers was bound, and for the first time allowed characterization of the, mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization, of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to, metallation and demethylation of N-MeMP. A mechanism of porphyrin, distortion is proposed, which assumes that the enzyme holds pyrrole rings, B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A.

Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at the terminal step of heme biosynthesis, was co-crystallized with an isomer mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray structure revealed the active site of the enzyme, to which only one of the isomers was bound, and for the first time allowed characterization of the mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to metallation and demethylation of N-MeMP. A mechanism of porphyrin distortion is proposed, which assumes that the enzyme holds pyrrole rings B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A.

==About this Structure==

1C1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and MMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1C1H OCA].

1C1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=MMP:'>MMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1H OCA].

==Reference==

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[[Category: rossmann fold]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 12:04:~~42 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:23 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1c1h.jpg|left|200px]]<br /><applet load="1c1h" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1c1h.jpg|left|200px]]<br /><applet load="1c1h" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1c1h, resolution 1.90&Aring;" />
 '''CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN'''<br />
 ==Overview==
-Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at, the terminal step of heme biosynthesis, was co-crystallized with an isomer, mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray, structure revealed the active site of the enzyme, to which only one of the, isomers was bound, and for the first time allowed characterization of the, mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization, of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to, metallation and demethylation of N-MeMP. A mechanism of porphyrin, distortion is proposed, which assumes that the enzyme holds pyrrole rings, B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A.
+Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at the terminal step of heme biosynthesis, was co-crystallized with an isomer mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray structure revealed the active site of the enzyme, to which only one of the isomers was bound, and for the first time allowed characterization of the mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to metallation and demethylation of N-MeMP. A mechanism of porphyrin distortion is proposed, which assumes that the enzyme holds pyrrole rings B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A.
 ==About this Structure==
-C1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and MMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C1H OCA].
+C1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=MMP:'>MMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1H OCA].
 ==Reference==
@@ Line 28: / Line 28: @@
 [[Category: rossmann fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:04:42 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:23 2008''