1lbq
From Proteopedia
(New page: 200px<br /><applet load="1lbq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lbq, resolution 2.4Å" /> '''The crystal structure...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1lbq.gif|left|200px]]<br /><applet load="1lbq" size=" | + | [[Image:1lbq.gif|left|200px]]<br /><applet load="1lbq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lbq, resolution 2.4Å" /> | caption="1lbq, resolution 2.4Å" /> | ||
'''The crystal structure of Saccharomyces cerevisiae ferrochelatase'''<br /> | '''The crystal structure of Saccharomyces cerevisiae ferrochelatase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ferrochelatase is the terminal enzyme in the heme biosynthetic pathway. It | + | Ferrochelatase is the terminal enzyme in the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into protoporphyrin IX to produce protoheme IX. The crystal structures of ferrochelatase from Saccharomyces cerevisiae in free form, in complex with Co(II), a substrate metal ion, and in complex with two inhibitors, Cd(II) and Hg(I), are presented in this work. The enzyme is a homodimer, with clear asymmetry between the monomers with regard to the porphyrin binding cleft and the mode of metal binding. The Co(II) and Cd(II) complexes reveal the metal binding site which consists of the invariant amino acids H235, E314, and S275 and solvent molecules. The shortest distance to the metal reveals that amino acid H235 is the primary metal binding residue. A second site with bound Cd(II) was found close to the surface of the molecule, approximately 14 A from H235, with E97, H317, and E326 participating in metal coordination. It is suggested that this site corresponds to the magnesium binding site in Bacillus subtilis ferrochelatase. The latter site is also located at the surface of the molecule and thought to be involved in initial metal binding and regulation. |
==About this Structure== | ==About this Structure== | ||
| - | 1LBQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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:// | + | 1LBQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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=1LBQ OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:26 2008'' |
Revision as of 11:43, 21 February 2008
|
The crystal structure of Saccharomyces cerevisiae ferrochelatase
Overview
Ferrochelatase is the terminal enzyme in the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into protoporphyrin IX to produce protoheme IX. The crystal structures of ferrochelatase from Saccharomyces cerevisiae in free form, in complex with Co(II), a substrate metal ion, and in complex with two inhibitors, Cd(II) and Hg(I), are presented in this work. The enzyme is a homodimer, with clear asymmetry between the monomers with regard to the porphyrin binding cleft and the mode of metal binding. The Co(II) and Cd(II) complexes reveal the metal binding site which consists of the invariant amino acids H235, E314, and S275 and solvent molecules. The shortest distance to the metal reveals that amino acid H235 is the primary metal binding residue. A second site with bound Cd(II) was found close to the surface of the molecule, approximately 14 A from H235, with E97, H317, and E326 participating in metal coordination. It is suggested that this site corresponds to the magnesium binding site in Bacillus subtilis ferrochelatase. The latter site is also located at the surface of the molecule and thought to be involved in initial metal binding and regulation.
About this Structure
1LBQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Ferrochelatase, with EC number 4.99.1.1 Full crystallographic information is available from OCA.
Reference
Metal binding to Saccharomyces cerevisiae ferrochelatase., Karlberg T, Lecerof D, Gora M, Silvegren G, Labbe-Bois R, Hansson M, Al-Karadaghi S, Biochemistry. 2002 Nov 19;41(46):13499-506. PMID:12427010
Page seeded by OCA on Thu Feb 21 13:43:26 2008
