1iaa: Difference between revisions

Revision as of 14:09, 21 February 2008

CRYSTAL STRUCTURES, SPECTROSCOPIC FEATURES, AND CATALYTIC PROPERTIES OF COBALT(II), COPPER(II), NICKEL(II), AND MERCURY(II) DERIVATIVES OF THE ZINC ENDOPEPTIDASE ASTACIN. A CORRELATION OF STRUCTURE AND PROTEOLYTIC ACTIVITY

OverviewOverview

The catalytic zinc ion of astacin, a prototypical metalloproteinase from crayfish, has been substituted by Co(II), Cu(II), Hg(II), and Ni(II) in order to probe the role of the metal for both catalysis and structure. Compared to Zn(II)-astacin, Co(II)- and Cu(II)-astacin display enzymatic activities of about 140 and 37%, respectively, while Ni(II)- and Hg(II)-astacin are almost inactive. The electron paramagnetic resonance spectrum of Cu(II)-astacin is typical of 5-fold coordinated copper(II), and its intense absorption maxima at 445 and 325 nm are probably due to ligand-metal charge-transfer transitions involving Tyr-149. This residue had been identified previously by x-ray crystallography of the zinc enzyme as a zinc ligand, in addition to three imidazoles and a glutamic acid-bound water molecule. We present now the refined high-resolution x-ray crystal structures of Cu(II)-, Co(II)-, and Ni(II)-astacin, which exhibit a virtually identical protein framework to the previously analyzed structures of Zn(II)-, apo-, and Hg(II)-astacin. In Co(II)- and Cu(II)-astacin, the metal is penta-coordinated similarly to the native zinc enzyme. In the Ni(II) derivative, however, an additional solvent molecule expands the metal coordination sphere to a distorted octahedral ligand geometry, while in Hg(II)-astacin, no ordered solvent molecule at all is observed in the inner coordination sphere of the metal. This indicates a close correlation between catalytic properties and ground-state metal coordination of astacin.

About this StructureAbout this Structure

1IAA is a Single protein structure of sequence from Astacus astacus with as ligand. Active as Astacin, with EC number 3.4.24.21 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures, spectroscopic features, and catalytic properties of cobalt(II), copper(II), nickel(II), and mercury(II) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity., Gomis-Ruth FX, Grams F, Yiallouros I, Nar H, Kusthardt U, Zwilling R, Bode W, Stocker W, J Biol Chem. 1994 Jun 24;269(25):17111-7. PMID:8006015

Page seeded by OCA on Thu Feb 21 13:09:41 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1iaa.gif|left|200px]]<br /><applet load="1iaa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1iaa.gif|left|200px]]<br /><applet load="1iaa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1iaa, resolution 1.90&Aring;" />
 '''CRYSTAL STRUCTURES, SPECTROSCOPIC FEATURES, AND CATALYTIC PROPERTIES OF COBALT(II), COPPER(II), NICKEL(II), AND MERCURY(II) DERIVATIVES OF THE ZINC ENDOPEPTIDASE ASTACIN. A CORRELATION OF STRUCTURE AND PROTEOLYTIC ACTIVITY'''<br />
 ==Overview==
-The catalytic zinc ion of astacin, a prototypical metalloproteinase from, crayfish, has been substituted by Co(II), Cu(II), Hg(II), and Ni(II) in, order to probe the role of the metal for both catalysis and structure., Compared to Zn(II)-astacin, Co(II)- and Cu(II)-astacin display enzymatic, activities of about 140 and 37%, respectively, while Ni(II)- and, Hg(II)-astacin are almost inactive. The electron paramagnetic resonance, spectrum of Cu(II)-astacin is typical of 5-fold coordinated copper(II), and its intense absorption maxima at 445 and 325 nm are probably due to, ligand-metal charge-transfer transitions involving Tyr-149. This residue, had been identified previously by x-ray crystallography of the zinc enzyme, as a zinc ligand, in addition to three imidazoles and a glutamic, acid-bound water molecule. We present now the refined high-resolution, x-ray crystal structures of Cu(II)-, Co(II)-, and Ni(II)-astacin, which, exhibit a virtually identical protein framework to the previously analyzed, structures of Zn(II)-, apo-, and Hg(II)-astacin. In Co(II)- and, Cu(II)-astacin, the metal is penta-coordinated similarly to the native, zinc enzyme. In the Ni(II) derivative, however, an additional solvent, molecule expands the metal coordination sphere to a distorted octahedral, ligand geometry, while in Hg(II)-astacin, no ordered solvent molecule at, all is observed in the inner coordination sphere of the metal. This, indicates a close correlation between catalytic properties and, ground-state metal coordination of astacin.
+The catalytic zinc ion of astacin, a prototypical metalloproteinase from crayfish, has been substituted by Co(II), Cu(II), Hg(II), and Ni(II) in order to probe the role of the metal for both catalysis and structure. Compared to Zn(II)-astacin, Co(II)- and Cu(II)-astacin display enzymatic activities of about 140 and 37%, respectively, while Ni(II)- and Hg(II)-astacin are almost inactive. The electron paramagnetic resonance spectrum of Cu(II)-astacin is typical of 5-fold coordinated copper(II), and its intense absorption maxima at 445 and 325 nm are probably due to ligand-metal charge-transfer transitions involving Tyr-149. This residue had been identified previously by x-ray crystallography of the zinc enzyme as a zinc ligand, in addition to three imidazoles and a glutamic acid-bound water molecule. We present now the refined high-resolution x-ray crystal structures of Cu(II)-, Co(II)-, and Ni(II)-astacin, which exhibit a virtually identical protein framework to the previously analyzed structures of Zn(II)-, apo-, and Hg(II)-astacin. In Co(II)- and Cu(II)-astacin, the metal is penta-coordinated similarly to the native zinc enzyme. In the Ni(II) derivative, however, an additional solvent molecule expands the metal coordination sphere to a distorted octahedral ligand geometry, while in Hg(II)-astacin, no ordered solvent molecule at all is observed in the inner coordination sphere of the metal. This indicates a close correlation between catalytic properties and ground-state metal coordination of astacin.
 ==About this Structure==
-IAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Astacus_astacus Astacus astacus] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Astacin Astacin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.21 3.4.24.21] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAA OCA].
+IAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Astacus_astacus Astacus astacus] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Astacin Astacin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.21 3.4.24.21] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAA OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Bode, W.]]
-[[Category: Gomis-Rueth, F.X.]]
+[[Category: Gomis-Rueth, F X.]]
 [[Category: Stoecker, W.]]
 [[Category: CU]]
 [[Category: zinc endopeptidase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:12:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:41 2008''