1iaa: Difference between revisions

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[[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 1.90Å" />

'''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==

1IAA 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].

1IAA 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:

[[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''

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@@ 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''