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(-) Description

Title :  CRYSTAL STRUCTURE OF SSO2452 FROM SULFOLOBUS SOLFATARICUS P2
 
Authors :  A. Mcrobbie, L. Carter, K. A. Johnson, M. Kerou, H. Liu, S. Mcmahon, M. Ok J. H. Naismith, M. F. White
Date :  19 Aug 08  (Deposition) - 19 May 09  (Release) - 13 Jul 11  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.00
Chains :  Asym./Biol. Unit :  A
Keywords :  Sso2452, Reca, Sulfolobus Solfataricus P2, Sspf, Unknown Function (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  A. M. Mcrobbie, L. G. Carter, M. Kerou, H. Liu, S. A. Mcmahon, K. A. Johnson, M. Oke, J. H. Naismith, M. F. White
Structural And Functional Characterisation Of A Conserved Archaeal Rada Paralog With Antirecombinase Activity.
J. Mol. Biol. V. 389 661 2009
PubMed-ID: 19414020  |  Reference-DOI: 10.1016/J.JMB.2009.04.060

(-) Compounds

Molecule 1 - SSO2452
    Chains: A
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Plasmid: PDEST14
    Expression System Taxid: 562
    Expression System Variant: BL21
    Fragment: RESIDUES 1-235
    Organism Scientific: SULFOLOBUS SOLFATARICUS P2
    Organism Taxid: 273057

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (2, 5)

Asymmetric/Biological Unit (2, 5)
No.NameCountTypeFull Name
1POP1Ligand/IonPYROPHOSPHATE 2-
2ZN4Ligand/IonZINC ION

(-) Sites  (5, 5)

Asymmetric Unit (5, 5)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREASP A:76 , GLU A:79 , HIS A:212 , HOH A:2094 , HOH A:2095BINDING SITE FOR RESIDUE ZN A 1236
2AC2SOFTWAREGLU A:197 , HIS A:199 , GLU A:218 , HOH A:2096BINDING SITE FOR RESIDUE ZN A 1237
3AC3SOFTWAREASP A:64 , HIS A:181BINDING SITE FOR RESIDUE ZN A 1238
4AC4SOFTWAREHIS A:215 , GLU A:234 , HOH A:2097BINDING SITE FOR RESIDUE ZN A 1239
5AC5SOFTWAREPRO A:32 , GLY A:33 , THR A:34 , GLY A:35 , LYS A:36 , THR A:37 , ILE A:38 , HOH A:2018 , HOH A:2098BINDING SITE FOR RESIDUE POP A 1240

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2W0M)

(-) Cis Peptide Bonds  (1, 1)

Asymmetric/Biological Unit
No.Residues
1Asp A:130 -Ser A:131

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2W0M)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 2W0M)

(-) Exons   (0, 0)

(no "Exon" information available for 2W0M)

(-) 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:220
 aligned with Q97VZ8_SULSO | Q97VZ8 from UniProtKB/TrEMBL  Length:262

    Alignment length:235
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150       160       170       180       190       200       210       220       230     
         Q97VZ8_SULSO     1 MVSRLSTGILDFDKLIQGGIPQGFFIALTGEPGTGKTIFSLHFIAKGLRDGDPCIYVTTEESRDSIIRQAKQFNWDFEEYIEKKLIIIDALMKEKEDQWSLVNLTPEELVNKVIEAKQKLGYGKARLVIDSVSALFLDKPAMARKISYYLKRVLNKWNFTIYATSQYAITTSQAFGFGVEHVADGIIRFRRMIRNGELHRYILIEKMRQTDHDKHVWEIDIVNGKGIVLKGRLEE 235
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ----KaiC-2w0mA01 A:5-234                                                                                                                                                                                                                  - Pfam domains
         Sec.struct. author ...ee...hhhhhhhhh..ee...eeeee.....hhhhhhhhhhhhhhhhh..eeeee...hhhhhhhhhhhh...hhhhh...eeeee...----........hhhhhhhhhhhhhhhhh...eeeeeehhhhhh..hhhhhhhhhhhhhhhhhhh.eeeeeee.-----------hhhhhh.eeeeeeeeee..eeeeeeeeeee.........eeeeee...eeeeeee... Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2w0m A   1 MVSRLSTGILDFDKLIQGGIPQGFFIALTGEPGTGKTIFSLHFIAKGLRDGDPCIYVTTEESRDSIIRQAKQFNWDFEEYIEKKLIIIDALM----DQWSLVNLTPEELVNKVIEAKQKLGYGKARLVIDSVSALFLDKPAMARKISYYLKRVLNKWNFTIYATSQ-----------GVEHVADGIIRFRRMIRNGELHRYILIEKMRQTDHDKHVWEIDIVNGKGIVLKGRLEE 235
                                    10        20        30        40        50        60        70        80        90 |    |100       110       120       130       140       150       160     |   -       180       190       200       210       220       230     
                                                                                                                      92   97                                                                  166         178
   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 2W0M)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2W0M)

(-) Pfam Domains  (1, 1)

Asymmetric/Biological Unit
(-)
Clan: P-loop_NTPase (1112)

(-) Gene Ontology  (12, 12)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (Q97VZ8_SULSO | Q97VZ8)
molecular function
    GO:0005524    ATP binding    Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
    GO:0008094    DNA-dependent ATPase activity    Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of single- or double-stranded DNA, and it drives another reaction.
    GO:0003690    double-stranded DNA binding    Interacting selectively and non-covalently with double-stranded DNA.
    GO:0004520    endodeoxyribonuclease activity    Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
    GO:0000400    four-way junction DNA binding    Interacting selectively and non-covalently with DNA containing four-way junctions, also known as Holliday junctions, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices.
    GO:0046872    metal ion binding    Interacting selectively and non-covalently with any metal ion.
    GO:0000150    recombinase activity    Catalysis of the identification and base-pairing of homologous sequences between single-stranded DNA and double-stranded DNA.
    GO:0003697    single-stranded DNA binding    Interacting selectively and non-covalently with single-stranded DNA.
biological process
    GO:0000730    DNA recombinase assembly    The aggregation, arrangement and bonding together of strand exchange proteins (recombinases) into higher order oligomers on single-stranded DNA.
    GO:0006312    mitotic recombination    The exchange, reciprocal or nonreciprocal, of genetic material between one DNA molecule and a homologous region of DNA that occurs during mitotic cell cycles.
    GO:0010212    response to ionizing radiation    Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ionizing radiation stimulus. Ionizing radiation is radiation with sufficient energy to remove electrons from atoms and may arise from spontaneous decay of unstable isotopes, resulting in alpha and beta particles and gamma rays. Ionizing radiation also includes X-rays.
    GO:0042148    strand invasion    The process in which the nucleoprotein complex (composed of the broken single-strand DNA and the recombinase) searches and identifies a region of homology in intact duplex DNA. The broken single-strand DNA displaces the like strand and forms Watson-Crick base pairs with its complement, forming a duplex in which each strand is from one of the two recombining DNA molecules.

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