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(-) Description

Title :  EUKARYOTIC TRANSLATION INITIATION FACTOR 5A FROM METHANOCOCCUS JANNASCHII
 
Authors :  K. K. Kim, L. W. Hung, H. Yokota, R. Kim, S. H. Kim
Date :  29 Jul 98  (Deposition) - 14 Oct 98  (Release) - 16 Nov 11  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.90
Chains :  Asym./Biol. Unit :  A
Keywords :  Initiation Factor, Eif-5A, Translation, Ob-Fold (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  K. K. Kim, L. W. Hung, H. Yokota, R. Kim, S. H. Kim
Crystal Structures Of Eukaryotic Translation Initiation Factor 5A From Methanococcus Jannaschii At 1. 8 A Resolution
Proc. Natl. Acad. Sci. Usa V. 95 10419 1998
PubMed-ID: 9724718  |  Reference-DOI: 10.1073/PNAS.95.18.10419
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - EUKARYOTIC TRANSLATION INITIATION FACTOR 5A
    Atcc: DSM 2661
    Cell Line: BL21
    Chains: A
    Collection: DSM 2661
    Engineered: YES
    Expression System: ESCHERICHIA COLI BL21(DE3)
    Expression System Plasmid: PET21A/PSJS1240
    Expression System Strain: BL21 (DE3)
    Expression System Taxid: 469008
    Organism Scientific: METHANOCALDOCOCCUS JANNASCHII
    Organism Taxid: 2190

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (0, 0)

(no "Ligand,Modified Residues,Ions" information available for 1EIF)

(-) Sites  (0, 0)

(no "Site" information available for 1EIF)

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 1EIF)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 1EIF)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 1EIF)

(-) PROSITE Motifs  (1, 1)

Asymmetric/Biological Unit (1, 1)
 PROSITEUniProtKBPDB
No.IDACDescriptionIDLocationCountLocation
1IF5A_HYPUSINEPS00302 Eukaryotic initiation factor 5A hypusine signature.IF5A_METJA35-42  1A:38-45

(-) Exons   (0, 0)

(no "Exon" information available for 1EIF)

(-) Sequences/Alignments

Asymmetric/Biological Unit
   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
(details for a mapped element are shown in a popup box when the mouse pointer rests over it) 
Chain A from PDB  Type:PROTEIN  Length:128
 aligned with IF5A_METJA | Q58625 from UniProtKB/Swiss-Prot  Length:132

    Alignment length:130
                                    10        20        30        40        50        60        70        80        90       100       110       120       130
           IF5A_METJA     1 MPGTKQVNVGSLKVGQYVMIDGVPCEIVDISVSKPGKHGGAKARVVGIGIFEKVKKEFVAPTSSKVEVPIIDRRKGQVLAIMGDMVQIMDLQTYETLELPIPEGIEGLEPGGEVEYIEAVGQYKITRVIG 130
               SCOP domains d1eifa1 A:4-73 Eukaryotic initiation   translation factor 5a (eIF5a)  d1eifa2 A:74-133                                             SCOP domains
               CATH domains 1eifA01 A:4-73  [code=2.30.30.30, no   name defined]                  1eifA02 A:74-133 Nucleic acid-binding proteins               CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ...eeeeehhh.....eeee..eeeeeeeeeee....--..eeeeeeee.....eeeeeee...eeeee..eeeeeeeeeee..eeeeee.....eeeee............eeeeeee..eeee.eeee Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------IF5A_HYP---------------------------------------------------------------------------------------- PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------- Transcript
                 1eif A   4 MPGTKQVNVGSLKVGQYVMIDGVPCEIVDISVSKPGK--GAKARVVGIGIFEKVKKEFVAPTSSKVEVPIIDRRKGQVLAIMGDMVQIMDLQTYETLELPIPEGIEGLEPGGEVEYIEAVGQYKITRVIG 133
                                    13        23        33      | 43        53        63        73        83        93       103       113       123       133
                                                               40 43
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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  (2, 2)

Asymmetric/Biological Unit
(-)
Class: All beta proteins (24004)

(-) CATH Domains  (2, 2)

Asymmetric/Biological Unit
(-)
Class: Mainly Beta (13760)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 1EIF)

(-) Gene Ontology  (10, 10)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (IF5A_METJA | Q58625)
molecular function
    GO:0003723    RNA binding    Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
    GO:0043022    ribosome binding    Interacting selectively and non-covalently with any part of a ribosome.
    GO:0003746    translation elongation factor activity    Functions in chain elongation during polypeptide synthesis at the ribosome.
    GO:0003743    translation initiation factor activity    Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.
biological process
    GO:0045901    positive regulation of translational elongation    Any process that activates or increases the frequency, rate or extent of translational elongation.
    GO:0045905    positive regulation of translational termination    Any process that activates or increases the frequency, rate or extent of translational termination.
    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.
    GO:0006452    translational frameshifting    A mechanism whereby different proteins may result from a single mRNA molecule, due to a change in the parsing of three nucleotides per codon relative to an initiating AUG codon.
    GO:0006413    translational initiation    The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
cellular component
    GO:0005737    cytoplasm    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

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        IF5A_METJA | Q58625: 2eif

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