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(-) Description

Title :  FUNCTIONAL CHARACTERIZATION OF PSEUDOMONAS AERUGINOSA PILF
 
Authors :  J. Koo
Date :  13 Jul 06  (Deposition) - 25 Jul 06  (Release) - 13 Jul 11  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.00
Chains :  Asym./Biol. Unit :  A,B
Keywords :  Pilf, Type Iv Pilus Biogenesis, Pseudomonas Aeruginosa, Tpr, Superhelix, Protein Binding (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  J. Koo, S. Tammam, S. Y. Ku, L. M. Sampaleanu, L. L. Burrows, P. L. Howell
Pilf Is An Outer Membrane Lipoprotein Required For Multimerization And Localization Of The Pseudomonas Aeruginosa Type Iv Pilus Secretin.
J. Bacteriol. V. 190 6961 2008
PubMed-ID: 18776008  |  Reference-DOI: 10.1128/JB.00996-08

(-) Compounds

Molecule 1 - TYPE 4 FIMBRIAL BIOGENESIS PROTEIN PILF
    Chains: A, B
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Plasmid: PET-28A
    Expression System Strain: B834
    Expression System Taxid: 562
    Expression System Vector Type: PLASMID
    Gene: PILF
    Organism Scientific: PSEUDOMONAS AERUGINOSA
    Organism Taxid: 208964
    Strain: PAO1

 Structural Features

(-) Chains, Units

  12
Asymmetric/Biological Unit : AB

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 6)

Asymmetric/Biological Unit (1, 6)
No.NameCountTypeFull Name
1MSE6Mod. Amino AcidSELENOMETHIONINE

(-) Sites  (0, 0)

(no "Site" information available for 2HO1)

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2HO1)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 2HO1)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2HO1)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 2HO1)

(-) Exons   (0, 0)

(no "Exon" information available for 2HO1)

(-) 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:222
 aligned with Q9HXJ2_PSEAE | Q9HXJ2 from UniProtKB/TrEMBL  Length:252

    Alignment length:222
                                    40        50        60        70        80        90       100       110       120       130       140       150       160       170       180       190       200       210       220       230       240       250  
        Q9HXJ2_PSEAE     31 KGRDEARDAYIQLGLGYLQRGNTEQAKVPLRKALEIDPSSADAHAALAVVFQTEMEPKLADEEYRKALASDSRNARVLNNYGGFLYEQKRYEEAYQRLLEASQDTLYPERSRVFENLGLVSLQMKKPAQAKEYFEKSLRLNRNQPSVALEMADLLYKEREYVPARQYYDLFAQGGGQNARSLLLGIRLAKVFEDRDTAASYGLQLKRLYPGSLEYQEFQAEK  252
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author .hhhhhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhh..hhhhhhhhhhhhhhh.hhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhh.hhhhhhhhhhhhh......hhhhhhhhhhhhhhhh.hhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhh.hhhhhhhhhhhhhh....hhhhhhhhhhhhhhh.hhhhhhhhhhhhhhhh..hhhhhhhhh.. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                2ho1 A   31 KGRDEARDAYIQLGLGYLQRGNTEQAKVPLRKALEIDPSSADAHAALAVVFQTEmEPKLADEEYRKALASDSRNARVLNNYGGFLYEQKRYEEAYQRLLEASQDTLYPERSRVFENLGLVSLQmKKPAQAKEYFEKSLRLNRNQPSVALEmADLLYKEREYVPARQYYDLFAQGGGQNARSLLLGIRLAKVFEDRDTAASYGLQLKRLYPGSLEYQEFQAEK  252
                                    40        50        60        70        80    |   90       100       110       120       130       140       150   |   160       170       180|      190       200       210       220       230       240       250  
                                                                                 85-MSE                                                              154-MSE                    181-MSE                                                                   


Chain B from PDB  Type:PROTEIN  Length:221
 aligned with Q9HXJ2_PSEAE | Q9HXJ2 from UniProtKB/TrEMBL  Length:252

    Alignment length:221
                                    41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201       211       221       231       241       251 
        Q9HXJ2_PSEAE     32 GRDEARDAYIQLGLGYLQRGNTEQAKVPLRKALEIDPSSADAHAALAVVFQTEMEPKLADEEYRKALASDSRNARVLNNYGGFLYEQKRYEEAYQRLLEASQDTLYPERSRVFENLGLVSLQMKKPAQAKEYFEKSLRLNRNQPSVALEMADLLYKEREYVPARQYYDLFAQGGGQNARSLLLGIRLAKVFEDRDTAASYGLQLKRLYPGSLEYQEFQAEK  252
               SCOP domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .hhhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhh.hhhhhhhhhhhhhhh...hhhhhhhhhhhhhhh.hhhhhhhhhhhhh......hhhhhhhhhhhhhhhh.hhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhh.hhhhhhhhhhhhhh....hhhhhhhhhhhhhhh.hhhhhhhhhhhhhhhh..hhhhhhhhhhh Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                2ho1 B 1032 GRDEARDAYIQLGLGYLQRGNTEQAKVPLRKALEIDPSSADAHAALAVVFQTEmEPKLADEEYRKALASDSRNARVLNNYGGFLYEQKRYEEAYQRLLEASQDTLYPERSRVFENLGLVSLQmKKPAQAKEYFEKSLRLNRNQPSVALEmADLLYKEREYVPARQYYDLFAQGGGQNARSLLLGIRLAKVFEDRDTAASYGLQLKRLYPGSLEYQEFQAEK 1252
                                  1041      1051      1061      1071      1081   |  1091      1101      1111      1121      1131      1141      1151  |   1161      1171      1181      1191      1201      1211      1221      1231      1241      1251 
                                                                              1085-MSE                                                             1154-MSE                   1181-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 2HO1)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2HO1)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 2HO1)

(-) Gene Ontology  (3, 3)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A,B   (Q9HXJ2_PSEAE | Q9HXJ2)
biological process
    GO:0009297    pilus assembly    The assembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies. Pili are variously involved in transfer of nucleic acids, adherence to surfaces, and formation of pellicles. Is required for bacterial conjugation, or can play a role in adherence to surfaces (when it is called a fimbrium), and in the formation of pellicles.
    GO:0046903    secretion    The controlled release of a substance by a cell or a tissue.
    GO:0043683    type IV pilus biogenesis    A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a type IV pilus. A type IV pilus is composed of a pilus fiber and approximately ten proteins at its base; type IV pili play a role in cell motility, adherence to substrates, and aggregation.

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 Related Entries

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UniProtKB/TrEMBL
        Q9HXJ2_PSEAE | Q9HXJ2: 2fi7

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