3ayh

From Proteopedia
Jump to navigation Jump to search

Crystal structure of the C17/25 subcomplex from S. pombe RNA Polymerase IIICrystal structure of the C17/25 subcomplex from S. pombe RNA Polymerase III

Structural highlights

3ayh is a 2 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.193Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPC9_SCHPO DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.[1]

Publication Abstract from PubMed

Eukaryotic RNA Polymerase III (Pol III) is a multi-subunit enzyme responsible for transcribing tRNA, 5S rRNA, and several small RNAs. Of the 17 subunits in Pol III, the C17 (Rpc17) and C25 (Rpc25) subunits form a stable subcomplex that protrudes from the core polymerase. In the present study, we determined the crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe. The subcomplex adopts an elongated shape, and each subunit has two domains. The two subunits in the subcomplex are tightly packed and extensively interact, with a contact area of 2,080 A(2) . The overall conformation of S. pombe C17/25 is considerably different from the previously reported structure of C17/25 from Saccharomyces cerevisiae, with respect to the position of the C17 HRDC domain, a helix-bundle essential for cell viability. In contrast, the S. pombe C17/25 structure is quite similar to those of the Pol II and archaeal counterparts, Rpb4/7 and RpoE/F, respectively, despite the low sequence similarity. A phylogenetic comparison of the C17 subunits among eukaryotes revealed that they can be classified into three groups, according to the length of the inter-domain linker. S. pombe C17, as well as Rpb4 and RpoF, belongs to the largest group, with the short linker. On the other hand, S. cerevisiae C17 belongs to the smallest group, with the long linker, which probably enables the subcomplex to assume the alternative conformation.

Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA Polymerase III.,Ehara H, Sekine SI, Yokoyama S Protein Sci. 2011 Jun 28. doi: 10.1002/pro.682. PMID:21714024[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Proshkina GM, Shematorova EK, Proshkin SA, Zaros C, Thuriaux P, Shpakovski GV. Ancient origin, functional conservation and fast evolution of DNA-dependent RNA polymerase III. Nucleic Acids Res. 2006 Jul 28;34(13):3615-24. Print 2006. PMID:16877568 doi:34/13/3615
  2. Ehara H, Sekine SI, Yokoyama S. Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA Polymerase III. Protein Sci. 2011 Jun 28. doi: 10.1002/pro.682. PMID:21714024 doi:10.1002/pro.682

3ayh, resolution 2.19Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA