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(-) Description

Title :  CRYSTAL STRUCTURE OF MS0666
 
Authors :  H. Wang, S. Kishishita, K. Murayama, T. Terada, M. Shirouzu, S. Yokoyama, Riken Structural Genomics/Proteomics Initiative (Rsgi)
Date :  12 Jul 06  (Deposition) - 12 Jan 07  (Release) - 24 Feb 09  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.70
Chains :  Asym./Biol. Unit :  A,B
Keywords :  Ph Domain, Protein Binding, Structural Genomics, Nppsfa, National Project On Protein Structural And Functional Analyses, Riken Structural Genomics/Proteomics Initiative, Rsgi (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  H. Wang, S. Kishishita, K. Murayama, T. Terada, M. Shirouzu, S. Yokoyama
Crystal Structure Of Ms0666
To Be Published
PubMed: search
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - RAL GUANINE NUCLEOTIDE EXCHANGE FACTOR RALGPS1A
    Chains: A, B
    Engineered: YES
    Expression System Plasmid: PX051128-20
    Expression System Vector Type: PLASMID
    Fragment: PLECKSTRIN HOMOLOGY DOMAIN
    Organism Common: HOUSE MOUSE
    Organism Scientific: MUS MUSCULUS
    Organism Taxid: 10090
    Other Details: CELL-FREE PROTEIN SYNTHESIS

 Structural Features

(-) Chains, Units

  12
Asymmetric/Biological Unit : AB

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 4)

Asymmetric/Biological Unit (1, 4)
No.NameCountTypeFull Name
1MSE4Mod. Amino AcidSELENOMETHIONINE

(-) Sites  (0, 0)

(no "Site" information available for 2DTC)

(-) SS Bonds  (0, 0)

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

(-) Cis Peptide Bonds  (0, 0)

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

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

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

(-) PROSITE Motifs  (0, 0)

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

(-) Exons   (0, 0)

(no "Exon" information available for 2DTC)

(-) 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:116
 aligned with RGPS1_MOUSE | A2AR50 from UniProtKB/Swiss-Prot  Length:585

    Alignment length:116
                                   469       479       489       499       509       519       529       539       549       559       569      
          RGPS1_MOUSE   460 PTMEGPLRRKTLLKEGRKPALSSWTRYWVVLSGATLLYYGAKSLRGTDRKHYKSTPGKKVSIVGWMVQLPDDPEHPDIFQLNNPDKGNVYKFQTGSRFHAILWHKHLDDACKSSRP 575
               SCOP domains -------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains -------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains -------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ..eeeeeeeeeee...........eeeeeeee..eeeeee.......hhhhh.....eeee....eee.........eeeee......eeeee..hhhhhhhhhhhhhhhhh.... Sec.struct. author
                 SAPs(SNPs) -------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE -------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript -------------------------------------------------------------------------------------------------------------------- Transcript
                 2dtc A   1 PTmEGPLRRKTLLKEGRKPALSSWTRYWVVLSGATLLYYGAKSLRGTDRKHYKSTPGKKVSIVGWmVQLPDDPEHPDIFQLNNPDKGNVYKFQTGSRFHAILWHKHLDDACKSSRP 116
                              |     10        20        30        40        50        60     |  70        80        90       100       110      
                              |                                                             66-MSE                                              
                              3-MSE                                                                                                             


Chain B from PDB  Type:PROTEIN  Length:115
 aligned with RGPS1_MOUSE | A2AR50 from UniProtKB/Swiss-Prot  Length:585

    Alignment length:115
                                   469       479       489       499       509       519       529       539       549       559       569     
          RGPS1_MOUSE   460 PTMEGPLRRKTLLKEGRKPALSSWTRYWVVLSGATLLYYGAKSLRGTDRKHYKSTPGKKVSIVGWMVQLPDDPEHPDIFQLNNPDKGNVYKFQTGSRFHAILWHKHLDDACKSSR 574
               SCOP domains ------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ..eeeeeeeeeee...........eeeeeeee..eeeeee.......hhhhh.....eeee....eee.........eeeee......eeeee..hhhhhhhhhhhhhhhhh... Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------- Transcript
                 2dtc B   1 PTmEGPLRRKTLLKEGRKPALSSWTRYWVVLSGATLLYYGAKSLRGTDRKHYKSTPGKKVSIVGWmVQLPDDPEHPDIFQLNNPDKGNVYKFQTGSRFHAILWHKHLDDACKSSR 115
                              |     10        20        30        40        50        60     |  70        80        90       100       110     
                              3-MSE                                                         66-MSE
   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 2DTC)

(-) CATH Domains  (0, 0)

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

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 2DTC)

(-) Gene Ontology  (9, 9)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A,B   (RGPS1_MOUSE | A2AR50)
molecular function
    GO:0008321    Ral guanyl-nucleotide exchange factor activity    Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Ral family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase.
    GO:0005085    guanyl-nucleotide exchange factor activity    Stimulates the exchange of guanyl nucleotides associated with a GTPase. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase.
biological process
    GO:0043547    positive regulation of GTPase activity    Any process that activates or increases the activity of a GTPase.
    GO:0032485    regulation of Ral protein signal transduction    Any process that modulates the frequency, rate or extent of Ral protein signal transduction.
    GO:0007264    small GTPase mediated signal transduction    Any series of molecular signals in which a small monomeric GTPase relays one or more of the signals.
cellular component
    GO:0005575    cellular_component    The part of a cell, extracellular environment or virus in which a gene product is located. A gene product may be located in one or more parts of a cell and its location may be as specific as a particular macromolecular complex, that is, a stable, persistent association of macromolecules that function together.
    GO:0005737    cytoplasm    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
    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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