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3j38

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Template:STRUCTURE 3j38

Contents

Structure of the D. melanogaster 40S ribosomal proteins

Function

[RS21_DROME] May be an associated component of the ribosome rather than a core structural subunit. May act as a translation initiation factor. Has a role in regulation of cell proliferation in the hematopoietic organs and the imaginal disks of larva.[1] [EF2_DROME] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. [RSSA_DROME] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Required during oogenesis and imaginal development.[2] [RS27A_DROME] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). Ribosomal protein S27a is a component of the 40S subunit of the ribosome. [RS2_DROME] Has a specific developmental role during oogenesis and a general role in protein synthesis as a component of the small ribosomal subunit.[3] [RS3_DROME] Has DNA repair activity directed towards the mutagenic lesions 8-oxoguanine and abasic sites in DNA. It can cleave DNA containing 8-oxoguanine residues efficiently. Also acts as an ap lyase, cleaving phosphodiester bonds via a beta,delta elimination reaction. [RS6_DROME] May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA. [RS3A_DROME] Essential for oogenesis; required for late follicle cell development.[4] [RS18_DROME] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315]

About this Structure

3j38 is a 35 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

  1. ↑ Torok I, Herrmann-Horle D, Kiss I, Tick G, Speer G, Schmitt R, Mechler BM. Down-regulation of RpS21, a putative translation initiation factor interacting with P40, produces viable minute imagos and larval lethality with overgrown hematopoietic organs and imaginal discs. Mol Cell Biol. 1999 Mar;19(3):2308-21. PMID:10022917
  2. ↑ Melnick MB, Noll E, Perrimon N. The Drosophila stubarista phenotype is associated with a dosage effect of the putative ribosome-associated protein D-p40 on spineless. Genetics. 1993 Oct;135(2):553-64. PMID:7916731
  3. ↑ Cramton SE, Laski FA. string of pearls encodes Drosophila ribosomal protein S2, has Minute-like characteristics, and is required during oogenesis. Genetics. 1994 Aug;137(4):1039-48. PMID:7982558
  4. ↑ Reynaud E, Bolshakov VN, Barajas V, Kafatos FC, Zurita M. Antisense suppression of the putative ribosomal protein S3A gene disrupts ovarian development in Drosophila melanogaster. Mol Gen Genet. 1997 Oct;256(4):462-7. PMID:9393444

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