Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion

Journal of Molecular Biology

Volumn 267, Issue 3, 1997, Pages 749-761

  Meinnel, Thierry ^a   Lazennec, Christine ^a   Villoing, Stéphane ^a   Blanquet, Sylvain ^a  

^a LABORATOIRE DE BIOCHIMIE   (France)

Author keywords

3D structure; Conserved motifs; Deformylase; Protein family; Therapeutic target

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; METALLOPROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; CONTROLLED STUDY; CYANOBACTERIUM; DATA BASE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ESCHERICHIA COLI; GEOBACILLUS STEAROTHERMOPHILUS; HAEMOPHILUS INFLUENZAE; LACTOCOCCUS LACTIS; MOLECULAR MODEL; MYCOPLASMA; MYCOPLASMA PNEUMONIAE; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; THERMUS THERMOPHILUS;

EID: 0031552348     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0904     Document Type: Article

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