 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](ek5022fig2mag.jpg)
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Figure 2
The SsoMCM-N dimer described in this work (a) has a subdomain architecture similar to that of the closed-ring structure (b) (PDB entry 2vl6; Liu et al., 2008  ). Adjacent subunits are arranged grossly similarly, including similar interactions of Ser114 with Asp191 and of Glu166 with Arg181 (noted with magenta boxes). The intersubunit interface of the dimer is tighter, with much more extensive interactions than in the closed-ring structure. The different proximities of the HB subdomains markedly distinguish the two types of interface. In particular, the dimer interface involves several residues of the HB subdomains, which do not interact at all in the closed-ring structure. Each panel illustrates chains A (yellow) and B (green) from each structure (top) and the interactions between the two chains (bottom). Hydrogen-bonding interactions are noted with purple dashes and salt-bridge interactions are noted with red dashes. Residues that contribute side-chain atoms to the interaction are shown with a solid outline and residues that contribute main-chain amide atoms are shown with a dashed outline. |
![[Figure 2]](ek5022fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
