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(-) Description

Title :  SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S27A FROM THERMOPLASMA ACIDOPHILUM
 
Authors :  B. Wu, A. Yee, C. Fares, A. Lemak, A. Semest, C. Arrowsmith, G. T. Monteli Northeast Structural Genomics Consortium (Nesg), Ontario Cen Structural Proteomics (Ocsp)
Date :  20 Jun 08  (Deposition) - 19 Aug 08  (Release) - 23 May 12  (Revision)
Method :  SOLUTION NMR
Resolution :  NOT APPLICABLE
Chains :  NMR Structure  :  A  (20x)
NMR Structure *:  A  (1x)
Keywords :  30S Ribosomal Protein S27A, Metal-Binding, Ribonucleoprotein, Ribosomal Protein, Zinc-Finger, Structural Genomics, Psi-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, Nesg, Ontario Centre For Structural Proteomics, Ocsp (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  B. Wu, A. Yee, C. Fares, A. Lemak, A. Semest, C. Arrowsmith
Solution Structure Of 30S Ribosomal Protein S27A From Thermoplasma Acidophilum/Northeast Structural Genomics Consortium Target Tat88/Ontario Center For Structural Proteomics Target Ta1093
To Be Published
PubMed: search
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - 30S RIBOSOMAL PROTEIN S27AE
    Chains: A
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Plasmid: P11
    Expression System Taxid: 562
    Expression System Vector Type: PLASMID
    Gene: RPS27AE, TA1093
    Organism Scientific: THERMOPLASMA ACIDOPHILUM
    Organism Taxid: 2303

 Structural Features

(-) Chains, Units

  1
NMR Structure (20x): A
NMR Structure * (1x): A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 1)

NMR Structure (1, 1)
No.NameCountTypeFull Name
1ZN1Ligand/IonZINC ION
NMR Structure * (0, 0)
No.NameCountTypeFull Name
1ZN-1Ligand/IonZINC ION

(-) Sites  (1, 1)

NMR Structure (1, 1)
No.NameEvidenceResiduesDescription
1AC1SOFTWARECYS A:21 , CYS A:39 , ARG A:41BINDING SITE FOR RESIDUE ZN A 56

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2K4X)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 2K4X)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2K4X)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 2K4X)

(-) Exons   (0, 0)

(no "Exon" information available for 2K4X)

(-) Sequences/Alignments

NMR Structure
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
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Chain A from PDB  Type:PROTEIN  Length:55
 aligned with RS27A_THEAC | Q9HJ78 from UniProtKB/Swiss-Prot  Length:55

    Alignment length:55
                                    10        20        30        40        50     
           RS27A_THEAC    1 MQKRELYEIADGKLVRKHRFCPRCGPGVFLAEHADRYSCGRCGYTEFKKAKKSKS 55
               SCOP domains d2k4xa1 A:1-55 Ribosomal protein S27ae                  SCOP domains
               CATH domains ------------------------------------------------------- CATH domains
               Pfam domains -Ribosomal_S27-2k4xA01 A:2-45                ---------- Pfam domains
         Sec.struct. author ..............................ee...eee.......ee........ Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------- Transcript
                  2k4x A  1 MQKRELYEIADGKLVRKHRFCPRCGPGVFLAEHADRYSCGRCGYTEFKKAKKSKS 55
                                    10        20        30        40        50
   Legend:   → Mismatch (orange background)
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  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (1, 1)

NMR Structure
(-)
Class: Small proteins (3458)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2K4X)

(-) Pfam Domains  (1, 1)

NMR Structure
(-)
Clan: Zn_Beta_Ribbon (109)

(-) Gene Ontology  (6, 6)

NMR Structure(hide GO term definitions)
Chain A   (RS27A_THEAC | Q9HJ78)
molecular function
    GO:0046872    metal ion binding    Interacting selectively and non-covalently with any metal ion.
    GO:0003735    structural constituent of ribosome    The action of a molecule that contributes to the structural integrity of the ribosome.
    GO:0008270    zinc ion binding    Interacting selectively and non-covalently with zinc (Zn) ions.
biological process
    GO:0006412    translation    The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
cellular component
    GO:0030529    intracellular ribonucleoprotein complex    An intracellular macromolecular complex containing both protein and RNA molecules.
    GO:0005840    ribosome    An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.

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