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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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