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Title :  CRYSTAL STRUCTURE OF MUTANT CYCLOPHILIN (R147A) FROM LEISHMANIA DONOVANI
 
Authors :  V. Venugopal, B. Sen, A. K. Datta, R. Banerjee
Date :  28 Dec 07  (Deposition) - 15 Jan 08  (Release) - 24 Feb 09  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.70
Chains :  Asym./Biol. Unit :  A
Keywords :  Cyclophilin, Rotamase, Proline, Isomerase, Cis-Trans, Protozoa, Leishmania, Donovani, Kala-Azar (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  V. Venugopal, B. Sen, A. K. Datta, R. Banerjee
Crystal Structure Of Mutant Cyclophilin From Leishmania Donovani
To Be Published
PubMed: search
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
    Chains: A
    EC Number: 5.2.1.8
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Plasmid: PQE32
    Expression System Strain: M15
    Expression System Taxid: 562
    Expression System Vector Type: PLASMID
    Fragment: UNP RESIDUES 22-187
    Mutation: YES
    Organism Scientific: LEISHMANIA DONOVANI
    Organism Taxid: 5661
    Synonym: CYCLOPHILIN

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (0, 0)

(no "Ligand,Modified Residues,Ions" information available for 3BT8)

(-) Sites  (0, 0)

(no "Site" information available for 3BT8)

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 3BT8)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 3BT8)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

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(-) PROSITE Motifs  (0, 0)

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(-) Exons   (0, 0)

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(-) Sequences/Alignments

Asymmetric/Biological Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
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SAPs(SNPs) PROSITE motifs Exons
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Chain A from PDB  Type:PROTEIN  Length:166
 aligned with Q9U9R3_LEIDO | Q9U9R3 from UniProtKB/TrEMBL  Length:187

    Alignment length:166
                                    31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181      
         Q9U9R3_LEIDO    22 EPEVTAKVYFDVMIDSEPLGRITIGLFGKDAPLTTENFRQLCTGEHGFGYKDSIFHRVIQNFMIQGGDFTNFDGTGGKSIYGEKFADENLNVKHFVGALSMANAGPNTNGSQFFITTAPTPWLDGRHVVFGKVLDGMDVVLRIEKTKTNSHDRPVKPVKIVASGEL 187
               SCOP domains d3bt8a_ A: automated matches                                                                                                                                           SCOP domains
               CATH domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .......eeeeee......eeeeeee....hhhhhhhhhhhhhh............eee...eeee...............................eeee...........eeee...hhhhh....eeeeeeehhhhhhhhh....hhhhh.....eeeeeee. Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ---------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3bt8 A  22 EPEVTAKVYFDVMIDSEPLGRITIGLFGKDAPLTTENFRQLCTGEHGFGYKDSIFHRVIQNFMIQGGDFTNFDGTGGKSIYGEKFADENLNVKHFVGALSMANAGPNTNGSQFFITTAPTPWLDGAHVVFGKVLDGMDVVLRIEKTKTNSHDRPVKPVKIVASGEL 187
                                    31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181
   Legend:   → Mismatch (orange background)
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  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: All beta proteins (24004)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 3BT8)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 3BT8)

(-) Gene Ontology  (4, 4)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (Q9U9R3_LEIDO | Q9U9R3)
molecular function
    GO:0016853    isomerase activity    Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
    GO:0003755    peptidyl-prolyl cis-trans isomerase activity    Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
biological process
    GO:0006457    protein folding    The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
    GO:0000413    protein peptidyl-prolyl isomerization    The modification of a protein by cis-trans isomerization of a proline residue.

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        Q9U9R3_LEIDO | Q9U9R3: 2haq 3eov 4s1e

(-) Related Entries Specified in the PDB File

2haq THE CRYSTAL STRUCTURE OF WILD TYPE CYCLOPHILIN FROM LEISHMANIA DONOVANI