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(-) Description

Title :  CRYSTAL STRUCTURE OF FTSY FROM MYCOPLASMA MYCOIDES- SPACE GROUP P21212
 
Authors :  T. Gariani, T. Samuelsson, A. E. Sauer-Eriksson
Date :  30 May 05  (Deposition) - 24 Jan 06  (Release) - 24 Feb 09  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.95
Chains :  Asym./Biol. Unit :  A
Keywords :  Gtpase, Ftsy, Signal Recognition Particle, Srp, Receptor, Protein Transport (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  T. Gariani, T. Samuelsson, A. E. Sauer-Eriksson
Conformational Variability Of The Gtpase Domain Of The Signal Recognition Particle Receptor Ftsy
J. Struct. Biol. V. 153 85 2006
PubMed-ID: 16343944  |  Reference-DOI: 10.1016/J.JSB.2005.10.003
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - FTSY
    Chains: A
    Engineered: YES
    Expression System: ESCHERICHIA COLI BL21(DE3)
    Expression System Plasmid: PET9D
    Expression System Strain: BL21(DE3)
    Expression System Taxid: 469008
    Expression System Vector Type: PLASMID
    Fragment: NG DOMAIN
    Organism Scientific: MYCOPLASMA MYCOIDES
    Organism Taxid: 2102
    Synonym: SRP RECEPTOR FTSY

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : A

Summary Information (see also Sequences/Alignments below)

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

Asymmetric/Biological Unit (1, 1)
No.NameCountTypeFull Name
1SO41Ligand/IonSULFATE ION

(-) Sites  (1, 1)

Asymmetric Unit (1, 1)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREASN A:205 , GLY A:206 , THR A:207 , GLY A:208 , LYS A:209 , THR A:210 , ARG A:236 , HOH A:1132BINDING SITE FOR RESIDUE SO4 A 1130

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 1ZU4)

(-) Cis Peptide Bonds  (1, 1)

Asymmetric/Biological Unit
No.Residues
1Ala A:318 -Pro A:319

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 1ZU4)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 1ZU4)

(-) Exons   (0, 0)

(no "Exon" information available for 1ZU4)

(-) 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:305
 aligned with FTSY_MYCMS | Q6MTB9 from UniProtKB/Swiss-Prot  Length:400

    Alignment length:309
                                    95       105       115       125       135       145       155       165       175       185       195       205       215       225       235       245       255       265       275       285       295       305       315       325       335       345       355       365       375       385         
           FTSY_MYCMS    86 KVEKAMLKSAFNFSKDIKKLSKKYKQADDEFFEELEDVLIQTDMGMKMVLKVSNLVRKKTKRDTSFENIKDALVESLYQAYTDNDWTNKKYRIDFKENRLNIFMLVGVNGTGKTTSLAKMANYYAELGYKVLIAAADTFRAGATQQLEEWIKTRLNNKVDLVKANKLNADPASVVFDAIKKAKEQNYDLLLIDTAGRLQNKVNLMAELEKMNKIIQQVEKSAPHEVLLVIDATTGQNGVIQAEEFSKVADVSGIILTKMDSTSKGGIGLAIKELLNIPIKMIGVGEKVDDLLAFDIDQYIVHLSSGFMQ 394
               SCOP domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author hhhhhhhhhhhhhhhhhhhhhhh....hhhhhhhhhhhhhhh..hhhhhhhhhhhhhhhh....hhhhhhhhhhhhhhhhhhh...----..........eeeeee.....hhhhhhhhhhhhhhhh...eeeee....hhhhhhhhhhhhh......eeee.......hhhhhhhhhhhhhhhh...eeeee...hhhhhhhhhhhhhhhhhhhhh.......eeeeeee...hhhhhhhhhhhh......eeeeehhhhh...hhhhhhhhhhh..eeeee.......eee.hhhhhhhhhhhhhh. Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 1zu4 A  97 PMEKAMLKSAFNFSKDIKKLSKKYKQADDEFFEELEDVLIQTDMGMKMVLKVSNLVRKKTKRDTSFENIKDALVESLYQAYTDNDW----YRIDFKENRLNIFMLVGVNGTGKTTSLAKMANYYAELGYKVLIAAADTFRAGATQQLEEWIKTRLNNKVDLVKANKLNADPASVVFDAIKKAKEQNYDLLLIDTAGRLQNKTNLMAELEKMNKIIQQVEKSAPHEVLLVIDATTGQNGVIQAEEFSKVADVSGIILTKMDSTSKGGIGLAIKELLNIPIKMIGVGEKVDDLLAFDIDQYIVHLSSGFMQ 405
                                   106       116       126       136       146       156       166       176     |   -|      196       206       216       226       236       246       256       266       276       286       296       306       316       326       336       346       356       366       376       386       396         
                                                                                                               182  187
   Legend:   → Mismatch (orange background)
  - → Gap (green background, '-', border residues have a numbering label)
    → Modified Residue (blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 1ZU4)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 1ZU4)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 1ZU4)

(-) Gene Ontology  (9, 9)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (FTSY_MYCMS | Q6MTB9)
molecular function
    GO:0005525    GTP binding    Interacting selectively and non-covalently with GTP, guanosine triphosphate.
    GO:0003924    GTPase activity    Catalysis of the reaction: GTP + H2O = GDP + phosphate.
    GO:0000166    nucleotide binding    Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
biological process
    GO:0006614    SRP-dependent cotranslational protein targeting to membrane    The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
    GO:0006612    protein targeting to membrane    The process of directing proteins towards a membrane, usually using signals contained within the protein.
cellular component
    GO:0005737    cytoplasm    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
    GO:0031226    intrinsic component of plasma membrane    The component of the plasma membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane.
    GO:0016020    membrane    A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
    GO:0005886    plasma membrane    The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

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 Related Entries

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

UniProtKB/Swiss-Prot
        FTSY_MYCMS | Q6MTB9: 1zu5

(-) Related Entries Specified in the PDB File

1zu5 THE SAME PROTEIN IN DIFFERENT SPACE GROUP, H32