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Structural features of the single-stranded DNA-binding protein MoSub1 from Magnaporthe oryzae
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A joint-team from China Agriculture University has gained insight into the mysterious structure and function of MoSub1, the Sub1 homology from rice blast fungus. Their research has been published on August 18th, 2012 in Acta Crystallogr D Biol Crystallogr.

MoSub1's 1.79 Å data were collected at 100 K on beamline station 3W1A at Beijing Synchrotron Research Facility (BSRF) and BL-17U at Shanghai Synchrotron Research Facility (SSRF).  MoSub1 forms a dimer in solution, and each monomer consists of an alpha helix and five β fold-lines. The structure of the protein shows high structure similarity with the structure of PC4 and has a similar dimer interface and DNA binding region to PC4, indicating that MoSub1 could bind DNA using the same motif as other proteins of the Sub1/PC4 family. MoSub1, like PC4, was able to bind single strand dT12 strongly with a Kd of 186 nM. Surprisingly, there are two novel features in the MoSub1 structure comparing PC4 C-terminal structure: a N-terminal to the DNA binding domain and a C-terminal extension. The N-terminal region to the DNA binding domain of MoSub1 turns back towards to the DNA binding site and may interact with DNA or DNA binding site directly. The C-terminal extension region, which is absent in PC4, may be capable of interacting with other protein partners instead of DNA.

The research provides the scientific community clues to understand the biological function of MoSub1 protein, synchrotron sources have helped the team to unveil the structure. "However, the C-terminal extension region of MoSub1 protein binds to different protein modules, and other complex structures are to be solved to dig out more interaction details, and more brilliant synchrotron beams would surely help to examine smaller crystals that we've already got." explains Prof. junfeng Liu, one of the team leades from China Agriculture university.


Jinguang Huang, Yanxiang Zhao, Dan Huang,Huaian Liu,Neil Justin, Wensheng Zhao, Junfeng Liu* and Youliang Peng.* Structural features of the single-stranded DNA-binding protein MoSub1 from Magnaporthe oryzae.Acta Cryst. (2012). D68, 1071–1076.

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