4AGH

Structural features of ssDNA binding protein MoSub1 from Magnaporthe oryzae

Summary for 4AGH

• Entry DOI: 10.2210/pdb4agh/pdb
• Descriptor: MOSUB1, TRANSCRIPTION COFACTOR (2 entities in total)
• Functional Keywords: transcription, ssdna binding protein
• Biological source: MAGNAPORTHE ORYZAE (RICE BLAST FUNGUS)
• Total number of polymer chains: 1
• Total formula weight: 16917.80

Authors

Huang, J.,Zhao, Y.,Huang, D.,liu, J.,Peng, Y. (deposition date: 2012-01-27, release date: 2012-08-29, Last modification date: 2024-05-08)

Primary citation

Huang, J.,Zhao, Y.,Huang, D.,Liu, H.,Justin, N.,Zhao, W.,Liu, J.,Peng, Y.
Structural Features of the Single-Stranded DNA-Binding Protein Mosub1 from Magnaporthe Oryzae.
Acta Crystallogr.,Sect.D, 68:1071-, 2012

PubMed Abstract: The well studied general transcription cofactor Sub1/PC4 has multiple functions in transcription. It plays both a negative and a positive role in transcription initiation and is involved in elongation and downstream transcription processes and as a transcription reinitiation factor. MoSub1, a Sub1/PC4 orthologue from rice blast fungus, binds the single-stranded DNA dT(12) tightly with an affinity of 186 nM. The crystal structure of MoSub1 has been solved to 1.79 Å resolution. The structure of the protein shows high similiarity to the structure of PC4 and it 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. There are two novel features in the MoSub1 structure: a region N-terminal to the DNA-binding domain and a C-terminal extension. The region N-terminal to the DNA-binding domain of MoSub1 turns back towards the DNA-binding site and may interact directly with DNA or the DNA-binding site. The C-terminal extension region, which is absent in PC4, may not be capable of interacting with DNA and is one possible reason for the differences between Sub1 and PC4.

PubMed: 22948907
DOI: 10.1107/S0907444912019932

Experimental method

X-RAY DIFFRACTION (1.787 Å)