Sandbox Reserved 1125: Difference between revisions
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The Zn ion which is involved in the catalytic activity is the Zn999. In a publication (http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2) which studies the catalytic domain of MMP8 thanks to the Pro-Leu-Gly-hydroxylamine inhibitor, this ion is penta-coordinated with: His197, His201 and His207 of MMP8 and with the carbonyl and the hydroxyl oxygen of the hydroxamic acid moiety of the inhibitor. | The Zn ion which is involved in the catalytic activity is the Zn999. In a publication (http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2) which studies the catalytic domain of MMP8 thanks to the Pro-Leu-Gly-hydroxylamine inhibitor, this ion is penta-coordinated with: His197, His201 and His207 of MMP8 and with the carbonyl and the hydroxyl oxygen of the hydroxamic acid moiety of the inhibitor. | ||
[[Image:ZN pocket interaction.gif | thumb|ZN pocket interaction]] | [[Image:ZN pocket interaction.gif | thumb|ZN pocket interaction]] | ||
The residues involved in the Zn interactions are one Asp residue (149) next to three His residues (147, 162 and 175). | The residues involved in the Zn interactions are one <scene name='71/719866/Zn998/1'>Asp residue (149) next to three His residues (147, 162 and 175)</scene>. | ||
This enzyme binds 2ZN ions per subunit. | This enzyme binds 2ZN ions per subunit. | ||
<font color='red'>maintain a Zn2+ atom coordinated with three water molecules. One of them is as well bound to the Glu residue thanks to a hydrogen bond. The second Zn2+ atom is not involved in the active site. At first, the Gly 206 residue of the substrate binds the active site thanks to the Zn2+ atom. When it binds it takes the place of unstable water molecules and establishes stabilizing interactions with the active site thanks to its C terminal part. Then, the Ala 182 residue of the enzyme makes a hydrogen bond with the NH group of the substrate: this allows the substrate to enter the cavity of the catalytic site. The rest of the protein is stabilized by 4 hydrogen bonds with the amino acid located in the cavity.</font> | <font color='red'>maintain a Zn2+ atom coordinated with three water molecules. One of them is as well bound to the Glu residue thanks to a hydrogen bond. The second Zn2+ atom is not involved in the active site. At first, the Gly 206 residue of the substrate binds the active site thanks to the Zn2+ atom. When it binds it takes the place of unstable water molecules and establishes stabilizing interactions with the active site thanks to its C terminal part. Then, the Ala 182 residue of the enzyme makes a hydrogen bond with the NH group of the substrate: this allows the substrate to enter the cavity of the catalytic site. The rest of the protein is stabilized by 4 hydrogen bonds with the amino acid located in the cavity.</font> | ||
