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چکیده
The solvent-accessible surfaces of the RWD-C domains of Ctf19 and Mcm21s have crystal lattice contacts with RWD-C domains of symmetry related Mcm21 and Ctf19 molecules, respectively. These interfaces include ~ 400–480 Å of buried surface area from each protein. The three different types of intermolecular contacts of Ctf19-Mcm21 complexes in the crystal are shown. A) Hydrophobic interactions involving helices α5 and α6 of Ctf19 (Val245, Ile248, Phe251, Leu252) and β5–β7 of Mcm21 (Leu235, Ile252, Ala250). B) Interactions between the two Ctf19-Mcm21 molecules in the crystallographic asymmetric unit. This contact includes mostly hydrophilic sidechains of amino acids from β3, β4, and α3 from Mcm21. C) Interactions mediated by the N-terminal RWD domain of two Ctf19s in the crystal.
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