Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair

Article Abstract:

A study was conducted to analyze the crystal structures of a 40 kDA ATPase fragment of Escherichia coli MutL complexed with a substrate analog and the product ADP. A search framework supporting the two domains of the LN40 apoprotein structure was utilized for the molecular replacement solution for the LN40-ADPnP structures. Results indicated that more than 60 disordered residues in the apoprotein structure become ordered and promote ADPnP binding and the dimerization of LN40.

Escherichia coli, Adenosine triphosphatase, Apoprotein, Apoproteins

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A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain

Article Abstract:

A study was conducted to analyze the binding of multiple ligands by the alpha-adaptin appendage domain. The cDNA encoding residues of mouse alpha-adaptin C was cloned in the vector pGEX 4T2 for production as an N-terminal fusion protein. Experimental results indicated a single pocket in the appendage domain to which different proteins implicated in endocytosis bind in the C-terminal subdomain.

Proteins, Ligands, Ligands (Chemistry)

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