Journal:JBIC:4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
<applet load="2l0u" size="600" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/3" align="right" caption="Solved Crystal Structure of Ferrochelatase Mutant"/>
+
<applet load="2l0u" size="450" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/3" align="right" caption="Solved Crystal Structure of Ferrochelatase Mutant"/>
=== Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase ===
=== Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase ===
<big>Mattias D. Hansson • Tobias Karlberg • Christopher A. G. So ̈derberg • Sreekanth Rajan • Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson</big><ref>DOI 10.1007/s00775-010-0720-4</ref>
<big>Mattias D. Hansson • Tobias Karlberg • Christopher A. G. So ̈derberg • Sreekanth Rajan • Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson</big><ref>DOI 10.1007/s00775-010-0720-4</ref>

Revision as of 12:27, 3 November 2013

Solved Crystal Structure of Ferrochelatase Mutant

Drag the structure with the mouse to rotate

Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase

Mattias D. Hansson • Tobias Karlberg • Christopher A. G. So ̈derberg • Sreekanth Rajan • Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson[1]


Molecular Tour

Ferrochelatase produces . It can also . However, the ability to insert other . In this way Bacillus subtilis ferrochelatase can insert copper into protoporphyrin IX, but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases prefer cobalt over copper. shows that , while A third residue, Tyr in B. subtilis, is a third ligand via a water molecule. Human and S. cerevisiae ferrochelatase utilizes In the structures of the ferrochelatases the Tyr/Met occupies the same position. We also know that the Tyr residue of the is a . By site directed mutagenesis and showed that the metal specificity changed so that the modified B. subtilis ferrochelatase . Two crystal structures are presented. how . The how a in the B. subtilis enzyme.

  1. Hansson MD, Karlberg T, Soderberg CA, Rajan S, Warren MJ, Al-Karadaghi S, Rigby SE, Hansson M. Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J Biol Inorg Chem. 2010 Nov 4. PMID:21052751 doi:10.1007/s00775-010-0720-4

Proteopedia Page Contributors and Editors (what is this?)

David Canner, Alexander Berchansky, Jaime Prilusky

This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
Personal tools