4o26

From Proteopedia

Jump to: navigation, search

Crystal structure of the TRBD domain of TERT and the CR4/5 of TR

Structural highlights

4o26 is a 4 chain structure with sequence from Oryzias latipes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.001Å
Ligands:SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TERT_ORYLA Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.[1] [2]

Publication Abstract from PubMed

Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR.

Structural basis for protein-RNA recognition in telomerase.,Huang J, Brown AF, Wu J, Xue J, Bley CJ, Rand DP, Wu L, Zhang R, Chen JJ, Lei M Nat Struct Mol Biol. 2014 Jun;21(6):507-12. doi: 10.1038/nsmb.2819. Epub 2014 May, 4. PMID:24793650[3]

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

Loading citation details..
No citations found

See Also

References

  1. Xie M, Mosig A, Qi X, Li Y, Stadler PF, Chen JJ. Structure and function of the smallest vertebrate telomerase RNA from teleost fish. J Biol Chem. 2008 Jan 25;283(4):2049-59. doi: 10.1074/jbc.M708032200. Epub 2007 , Nov 26. PMID:18039659 doi:http://dx.doi.org/10.1074/jbc.M708032200
  2. Bley CJ, Qi X, Rand DP, Borges CR, Nelson RW, Chen JJ. RNA-protein binding interface in the telomerase ribonucleoprotein. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20333-8. doi: , 10.1073/pnas.1100270108. Epub 2011 Nov 28. PMID:22123986 doi:http://dx.doi.org/10.1073/pnas.1100270108
  3. Huang J, Brown AF, Wu J, Xue J, Bley CJ, Rand DP, Wu L, Zhang R, Chen JJ, Lei M. Structural basis for protein-RNA recognition in telomerase. Nat Struct Mol Biol. 2014 Jun;21(6):507-12. doi: 10.1038/nsmb.2819. Epub 2014 May, 4. PMID:24793650 doi:http://dx.doi.org/10.1038/nsmb.2819

Contents


PDB ID 4o26

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools