Sandbox Reserved 1125: Difference between revisions

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=== Catalytic domain ===

Thanks to X-ray crystallography, the catalytic domain structure has been solved with 1,7 Å resolution (2OY4).This domain is composed of 157 residues, from Met86 to Gly242, organized in <scene name='71/719866/Helixes/3'>three alpha helixes</scene> and <scene name='71/719866/Sheets/2'>five beta sheets</scene>.The protein folding and especially the zinc environment of the collagenase catalytic domain is very close to the astacins and the snake venom metalloproteinases. The catalytic domain alone has proteolytic activity against other protein substrates and synthetic substrates.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2]

Thanks to X-ray crystallography, the catalytic domain structure has been solved with 1,7 Å resolution (2OY4).This domain is composed of 157 residues, from Met86 to Gly242, organized in <scene name='71/719866/Helixes/4'>three alpha helixes</scene> and <scene name='71/719866/Sheets/3'>five beta sheets</scene>.The protein folding and especially the zinc environment of the collagenase catalytic domain is very close to the astacins and the snake venom metalloproteinases. The catalytic domain alone has proteolytic activity against other protein substrates and synthetic substrates.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2]

==== Ca2+ interactions ====

[[Image:CA_pocket_interaction.gif | thumb|CA996 pocket interaction]]This enzyme binds 3 Ca ions, 2 of them in the catalytic domain, which are packed against the top of the beta sheet and mostly have a structural function, stabilizing the catalytic domain.

Sandbox Reserved 1125: Difference between revisions

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@@ Line 32: / Line 32: @@
 === Catalytic domain ===
-Thanks to X-ray crystallography, the catalytic domain structure has been solved with 1,7 Å resolution (2OY4).This domain is composed of 157 residues, from Met86 to Gly242, organized in <scene name='71/719866/Helixes/3'>three alpha helixes</scene> and <scene name='71/719866/Sheets/2'>five beta sheets</scene>.The protein folding and especially the zinc environment of the collagenase catalytic domain is very close to the astacins and the snake venom metalloproteinases. The catalytic domain alone has proteolytic activity against other protein substrates and synthetic substrates.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2]
+Thanks to X-ray crystallography, the catalytic domain structure has been solved with 1,7 Å resolution (2OY4).This domain is composed of 157 residues, from Met86 to Gly242, organized in <scene name='71/719866/Helixes/4'>three alpha helixes</scene> and <scene name='71/719866/Sheets/3'>five beta sheets</scene>.The protein folding and especially the zinc environment of the collagenase catalytic domain is very close to the astacins and the snake venom metalloproteinases. The catalytic domain alone has proteolytic activity against other protein substrates and synthetic substrates.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2]
 ==== Ca2+ interactions ====
 [[Image:CA_pocket_interaction.gif | thumb|CA996 pocket interaction]]This enzyme binds 3 Ca ions, 2 of them in the catalytic domain, which are packed against the top of the beta sheet and mostly have a structural function, stabilizing the catalytic domain.