4pck | pdb_00004pck

Crystal structure of the P22S mutant of N-terminal CS domain of human Shq1

spinqualitylabelsall models 4pck, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pck is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.401Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SHQ1_HUMAN Required for the quantitative accumulation of H/ACA ribonucleoproteins (RNPs), including telomerase, probably through the stabilization of DKC1, from the time of its synthesis until its association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA. Publication Abstract from PubMed Shq1 is an essential protein involved in the early steps of biogenesis and assembly of H/ACA RNPs. Shq1 binds to dyskerin (Cbf5 in yeast) at an early step of H/ACA RNP assembly and is subsequently displaced by the H/ACA RNA. Shq1 contains an N-terminal CS and a C-terminal Shq1-specific domain (SSD). Dyskerin harbors many dyskeratosis congenita (DC) associated mutations. Structures of yeast Shq1 SSD bound to Cbf5 revealed that only a subset of these mutations is in the SSD binding site, implicating another subset in the putative CS binding site. Here we present the crystal structure of human Shq1 CS (hCS) and the NMR and crystal structure of hCS containing a serine substitution for proline 22 that is associated with some prostate cancers. The structure of hCS is similar to yeast Shq1 CS domain (yCS) and consists of two beta-sheets that form an immunoglobulin-like beta-sandwich fold. The N-terminal affinity tag sequence AHHHHHH associates with a neighboring protein in the crystal lattice to form an extra beta-strand. Deletion of this tag was required to get spectra suitable for NMR structure determination, while the tag was required for crystallization. NMR chemical shift perturbation (CSP) experiments with dyskerin and Cbf5 derived peptides from putative CS binding sites revealed a conserved surface on CS important for Cbf5/dyskerin binding. A HADDOCK docking model of a Shq1-Cbf5 complex that defines the position of CS domain in the pre-H/ACA RNP was calculated using the CSP data. Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1.,Singh M, Wang Z, Cascio D, Feigon J J Mol Biol. 2014 Dec 29. pii: S0022-2836(14)00646-9. doi:, 10.1016/j.jmb.2014.12.012. PMID:25553844 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA