Amicyanin
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
The 3D structure of ACY shows that the protein assumes a β-sandwich topology. The Cu+2 binding site has tetragonal geometry with interactions to 2 His, Cys and Met side chains. ACY interacts with methylamine dehydrogenase via a hydrophobic patch and Arg salt bridge<ref>PMID:21268585</ref>. | The 3D structure of ACY shows that the protein assumes a β-sandwich topology. The Cu+2 binding site has tetragonal geometry with interactions to 2 His, Cys and Met side chains. ACY interacts with methylamine dehydrogenase via a hydrophobic patch and Arg salt bridge<ref>PMID:21268585</ref>. | ||
| + | ==3D structures of amicyanin== | ||
| + | [[Amicyanin 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
Revision as of 07:12, 9 August 2022
| |||||||||||
References
- ↑ Zhu Z, Cunane LM, Chen Z, Durley RC, Mathews FS, Davidson VL. Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin. Biochemistry. 1998 Dec 8;37(49):17128-36. PMID:9860825 doi:10.1021/bi9817919
- ↑ Choi M, Sukumar N, Mathews FS, Liu A, Davidson VL. Proline 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein-Protein Interface. Biochemistry. 2011 Jan 26. PMID:21268585 doi:10.1021/bi101794y
