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(-) Description

Title :  STRUCTURE OF THE DIHYDROFOLATE REDUCTASE (FOLA) FROM COXIELLA BURNETII IN COMPLEX WITH METHOTREXATE
 
Authors :  M. C. Franklin, M. Cassidy, B. Hillerich, J. Love
Date :  09 Sep 11  (Deposition) - 02 Nov 11  (Release) - 20 Jan 16  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.30
Chains :  Asym./Biol. Unit :  A
Keywords :  Dihydrofolate Reductase, Oxidoreductase-Oxidoreductase Inhibitor Complex (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

Molecule 1 - DIHYDROFOLATE REDUCTASE
    Chains: A
    EC Number: 1.5.1.3
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Plasmid: PET
    Expression System Taxid: 562
    Expression System Vector Type: PLASMID
    Gene: CBU_1993, FOLA
    Organism Scientific: COXIELLA BURNETII
    Organism Taxid: 777
    Strain: RSA 493 NINE MILE PHASE I

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : A

Summary Information (see also Sequences/Alignments below)

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

Asymmetric/Biological Unit (2, 2)
No.NameCountTypeFull Name
1MTX1Ligand/IonMETHOTREXATE
2NDP1Ligand/IonNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDEPHOSPHATE

(-) Sites  (2, 2)

Asymmetric Unit (2, 2)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREALA A:7 , ALA A:8 , ILE A:15 , GLY A:16 , ARG A:17 , ASN A:19 , GLU A:20 , GLY A:44 , ARG A:45 , ARG A:46 , THR A:47 , SER A:50 , ILE A:63 , THR A:64 , GLN A:65 , GLN A:66 , TYR A:78 , ILE A:96 , GLY A:98 , ALA A:99 , ARG A:100 , ILE A:101 , GLU A:104 , VAL A:125 , MTX A:2001BINDING SITE FOR RESIDUE NDP A 1001
2AC2SOFTWAREILE A:6 , ALA A:7 , ALA A:8 , LEU A:21 , ASP A:28 , LEU A:29 , PHE A:32 , LYS A:33 , SER A:50 , ILE A:51 , ARG A:58 , ILE A:96 , THR A:115 , NDP A:1001BINDING SITE FOR RESIDUE MTX A 2001

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 3TQ9)

(-) Cis Peptide Bonds  (1, 1)

Asymmetric/Biological Unit
No.Residues
1Gly A:97 -Gly A:98

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 3TQ9)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 3TQ9)

(-) Exons   (0, 0)

(no "Exon" information available for 3TQ9)

(-) 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:151
 aligned with Q83AB2_COXBU | Q83AB2 from UniProtKB/TrEMBL  Length:161

    Alignment length:160
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150       160
         Q83AB2_COXBU     1 MIITLIAAMDKNRLIGRNNELPWHLPADLAHFKSITLGKPIVMGRRTFDSIGKPLPHRRNIVITQQKNLIIEGCDIFYSLDDALSALTKEPEVIIIGGARIFKEALPKADKMILTIINHSFEGDVYFPEWNDKEWKITSQIKHERDEKNPYPFQFLELRR 160
               SCOP domains d3tq9a_ A: automated matches                                                                                                                                     SCOP domains
               CATH domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .eeeeeeeee...eee........hhhhhhhhhhhhh..eeeeehhhhhhhh......eeeee..........eeee.hhhhhhhhh....eeeeeehhhhhhhhhhhh.eeeeeee.......ee....hhhhheeeeee..---------..eeeee. Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ---------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3tq9 A   1 MIITLIAAMDKNRLIGRNNELPWHLPADLAHFKSITLGKPIVMGRRTFDSIGKPLPHRRNIVITQQKNLIIEGCDIFYSLDDALSALTKEPEVIIIGGARIFKEALPKADKMILTIINHSFEGDVYFPEWNDKEWKITSQIKH---------FQFLELRR 160
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140  |      -  |    160
                                                                                                                                                                        143       153
   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  (1, 1)

Asymmetric/Biological Unit
(-)
Class: Alpha and beta proteins (a/b) (23833)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 3TQ9)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 3TQ9)

(-) Gene Ontology  (9, 9)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (Q83AB2_COXBU | Q83AB2)
molecular function
    GO:0050661    NADP binding    Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
    GO:0004146    dihydrofolate reductase activity    Catalysis of the reaction: 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+.
    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.
    GO:0016491    oxidoreductase activity    Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
biological process
    GO:0006545    glycine biosynthetic process    The chemical reactions and pathways resulting in the formation of glycine, aminoethanoic acid.
    GO:0009165    nucleotide biosynthetic process    The chemical reactions and pathways resulting in the formation of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates).
    GO:0006730    one-carbon metabolic process    The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
    GO:0055114    oxidation-reduction process    A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
    GO:0046654    tetrahydrofolate biosynthetic process    The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

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 Related Entries

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

UniProtKB/TrEMBL
        Q83AB2_COXBU | Q83AB2: 3tq8 3tqa 3tqb

(-) Related Entries Specified in the PDB File

3tq8 3tqa 3tqb