4agh | pdb_00004agh

Structural features of ssDNA binding protein MoSub1 from Magnaporthe oryzae

spinqualitylabelsall models 4agh, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4agh is a 1 chain structure with sequence from Magor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A 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. Structural features of the single-stranded DNA-binding protein MoSub1 from Magnaporthe oryzae.,Huang J, Zhao Y, Huang D, Liu H, Justin N, Zhao W, Liu J, Peng Y Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1071-6. Epub 2012 Aug 18. PMID:22948907 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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