2h1v: Difference between revisions

Revision as of 18:37, 21 February 2008

Crystal structure of the Lys87Ala mutant variant of Bacillus subtilis ferrochelatase

OverviewOverview

Ferrochelatase catalyzes the terminal step in the heme biosynthetic pathway, i.e., the incorporation of Fe(II) into protoporphyrin IX. Various biochemical and biophysical methods have been used to probe the enzyme for metal binding residues and the location of the active site. However, the location of the metal binding site and the path of the metal into the porphyrin are still disputed. Using site-directed mutagenesis on Bacillus subtilis ferrochelatase we demonstrate that exchange of the conserved residues His183 and Glu264 affects the metal affinity of the enzyme. We also present the first X-ray crystal structure of ferrochelatase with iron. Only a single iron was found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron was not present in the structure of a His183Ala modified ferrochelatase. The results strongly suggest that the insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264.

About this StructureAbout this Structure

2H1V is a Single protein structure of sequence from Bacillus subtilis with as ligand. Active as Ferrochelatase, with EC number 4.99.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX., Hansson MD, Karlberg T, Rahardja MA, Al-Karadaghi S, Hansson M, Biochemistry. 2007 Jan 9;46(1):87-94. PMID:17198378

Page seeded by OCA on Thu Feb 21 17:37:22 2008

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OCA

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-[[Image:2h1v.gif|left|200px]]<br /><applet load="2h1v" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2h1v.gif|left|200px]]<br /><applet load="2h1v" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2h1v, resolution 1.20&Aring;" />
 '''Crystal structure of the Lys87Ala mutant variant of Bacillus subtilis ferrochelatase'''<br />
 ==Overview==
-Ferrochelatase catalyzes the terminal step in the heme biosynthetic, pathway, i.e., the incorporation of Fe(II) into protoporphyrin IX. Various, biochemical and biophysical methods have been used to probe the enzyme for, metal binding residues and the location of the active site. However, the, location of the metal binding site and the path of the metal into the, porphyrin are still disputed. Using site-directed mutagenesis on Bacillus, subtilis ferrochelatase we demonstrate that exchange of the conserved, residues His183 and Glu264 affects the metal affinity of the enzyme. We, also present the first X-ray crystal structure of ferrochelatase with, iron. Only a single iron was found in the active site, coordinated in a, square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron was not present in the structure of a, His183Ala modified ferrochelatase. The results strongly suggest that the, insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs, from a metal binding site represented by His183 and Glu264.
+Ferrochelatase catalyzes the terminal step in the heme biosynthetic pathway, i.e., the incorporation of Fe(II) into protoporphyrin IX. Various biochemical and biophysical methods have been used to probe the enzyme for metal binding residues and the location of the active site. However, the location of the metal binding site and the path of the metal into the porphyrin are still disputed. Using site-directed mutagenesis on Bacillus subtilis ferrochelatase we demonstrate that exchange of the conserved residues His183 and Glu264 affects the metal affinity of the enzyme. We also present the first X-ray crystal structure of ferrochelatase with iron. Only a single iron was found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron was not present in the structure of a His183Ala modified ferrochelatase. The results strongly suggest that the insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264.
 ==About this Structure==
-H1V 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2H1V OCA].
+H1V 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2H1V OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Al-Karadaghi, S.]]
 [[Category: Hansson, M.]]
-[[Category: Hansson, M.D.]]
+[[Category: Hansson, M D.]]
 [[Category: Karlberg, T.]]
-[[Category: Rahardja, M.Arys.]]
+[[Category: Rahardja, M Arys.]]
 [[Category: MG]]
 [[Category: pi-helix]]
 [[Category: rossman fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:30:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:22 2008''