Succinyl-CoA synthetase
From Proteopedia
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| - | <applet load= | + | <applet load='1cqj' size='300' frame='true' align='right' caption='Structure of succinyl-CoA synthetase' /> |
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'''Succinyl-Coa synthetase''' catalyzes the reversible reaction of succinyl-CoA + ADP + Pi <-> succinate + CoA + ATP. | '''Succinyl-Coa synthetase''' catalyzes the reversible reaction of succinyl-CoA + ADP + Pi <-> succinate + CoA + ATP. | ||
==Structure== | ==Structure== | ||
| - | '''Succinyl-CoA synthetase''' | + | '''Succinyl-CoA synthetase''' is a tetramer with an active site on each dimer. This can be seen in the Jmol representation (the PDB code is 1CQJ). |
| - | The B chain consists of <scene name='Serine_Protease/Domains/1'>two domains</scene>. As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel. The specificity pocket (here filled with the Lys sidechain of the PPACK inhibitor) is in one side of the throat of the domain 2beta barrel, and the activation site is close next to it. | ||
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| - | <applet load="2ptc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="Trypsin BPT1 complex" /> | ||
==Trypsin-BPTI complex== | ==Trypsin-BPTI complex== | ||
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{{Clear}} | {{Clear}} | ||
== '''Content Donators''' == | == '''Content Donators''' == | ||
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| - | * Content for this page has been included and adapted with permission from Jane S. and David C. Richardson's http://kinemage.biochem.duke.edu/ | ||
Revision as of 07:45, 28 February 2010
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Succinyl-Coa synthetase catalyzes the reversible reaction of succinyl-CoA + ADP + Pi <-> succinate + CoA + ATP.
Structure
Succinyl-CoA synthetase is a tetramer with an active site on each dimer. This can be seen in the Jmol representation (the PDB code is 1CQJ).
Trypsin-BPTI complex
The trypsin backbone is shown in pink and the trypsin inhibitor, BPTI, in yellow (PDB code 2ptc). The residues [Ser195-His57-Asp102-Ser214] are shown in green, the disulfide bond between residues 14-38 is shown in yellow and the Lys 15 sidechain at the specificity site in pink.
Content Donators
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Lucas Hamlow, J.D. McClintic, Wayne Decatur, David Canner, Alexander Berchansky
