1c9e: Difference between revisions

Line 1:

[[Image:1c9e.~~gif~~|left|200px]]

[[Image:1c9e.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE~~'''~~

===STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10704318}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10704318 is the PubMed ID number.

-->

==About this Structure==

Line 34:

Line 38:

[[Category: N-methylmesoporphyrin]]

[[Category: Porphyrin metallation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:29:30 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:24:09 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1c9e.gif|left|200px]]
+{{Seed}}
+[[Image:1c9e.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1c9e|  PDB=1c9e  |  SCENE=  }}
-'''STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE'''
+===STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10704318}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10704318 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10704318}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: N-methylmesoporphyrin]]
 [[Category: Porphyrin metallation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:29:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:24:09 2008''