3TRE - JenaLib

Title :   STRUCTURE OF A TRANSLATION ELONGATION FACTOR P (EFP) FROM COXIELLA BURNETII

Authors :   J. Cheung, M. C. Franklin, M. Rudolph, M. Cassidy, E. Gary, F. Burshteyn

Date :   09 Sep 11 (Deposition) - 28 Sep 11 (Release) - 20 Jan 16 (Revision)

Method :   X-RAY DIFFRACTION

Resolution :   2.90

Chains :   Asym./Biol. Unit : A

Keywords :   Protein Synthesis, Translation (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   M. C. Franklin, J. Cheung, M. J. Rudolph, F. Burshteyn, M. Cassidy, E. Gary, B. Hillerich, Z. K. Yao, P. R. Carlier, M. Totrov, J. D. Love
Structural Genomics For Drug Design Against The Pathogen Coxiella Burnetii.
Proteins V. 83 2124 2015
PubMed-ID: 26033498 | Reference-DOI: 10.1002/PROT.24841

Compounds

Structural Features

Chains, Units

Ligands, Modified Residues, Ions (1, 5)

Sites (0, 0)

SS Bonds (0, 0)

Cis Peptide Bonds (0, 0)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

PROSITE Motifs (0, 0)

Exons (0, 0)

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

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Chain A from PDB  Type:PROTEIN  Length:129
 aligned with EFP_COXBU | Q83AR4 from UniProtKB/Swiss-Prot  Length:188

    Alignment length:129
                                    12        22        32        42        52        62        72        82        92       102       112       122         
            EFP_COXBU     3 THSTNEFRGGLKVMVDGDPCSIIDNEFVKPGKGQAFNRVKFRNLKTGRVLERTFKSGETLPAADVVEVEMQYLYNDGEFWHFMTSENYEQHAASKEAVAEAKQWLKEEALCMVTMWNGVPLSVEPPNFV 131
               SCOP domains d3trea1 A:3-65 automated matches                               d3trea2 A:66-131 automated matches                                 SCOP domains
               CATH domains --------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .ee.hhh....eeee..eeeeeeeeeee.......eeeeeeee.....eeeeeee...ee....eeeeeeeeeee....eeeee.....eeeehhhhhhhhhhhh....eeeeeee..eeeeee..... Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE --------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript --------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3tre A   3 THSTNEFRGGLKVmVDGDPCSIIDNEFVKPGKGQAFNRVKFRNLKTGRVLERTFKSGETLPAADVVEVEmQYLYNDGEFWHFmTSENYEQHAASKEAVAEAKQWLKEEALCmVTmWNGVPLSVEPPNFV 131
                                    12   |    22        32        42        52        62        72        82  |     92       102       112 |  |  122         
                                        16-MSE                                                  72-MSE       85-MSE                      114-MSE             
                                                                                                                                            117-MSE

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Classification and Annotation

SCOP Domains (2, 2)

CATH Domains (0, 0)

Pfam Domains (0, 0)

Gene Ontology (5, 5)

Asymmetric/Biological Unit(hide GO term definitions)

Chain A (EFP_COXBU | Q83AR4)

molecular function
	GO:0003746	translation elongation factor activity	Functions in chain elongation during polypeptide synthesis at the ribosome.
biological process
	GO:0043043	peptide biosynthetic process	The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide.
	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:0006414	translational elongation	The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.
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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Description