The 1.9 Å crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site

Biochemistry

Volumn 44, Issue 5, 2005, Pages 1471-1481

  LeMagueres, Pierre ^a   Im, Hookang ^a   Ebalunode, Jerry ^a   Strych, Ulrich ^a   Benedik, Michael J ^b   Briggs, James M ^a   Kohn, Harold ^c   Krause, Kurt L ^a,d  

^a University of Houston   (United States)

^b TEXAS A AND M UNIVERSITY   (United States)

^c UNIVERSITY OF NORTH CAROLINA   (United States)

^d BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CRYSTALLOGRAPHY; DIMERS; DISEASES; MONOMERS; SUBSTRATES;

ALANINE RACEMASE; STRUCTURE-AIDED DRUG DESIGN; TUBERCULOSIS;

CRYSTAL STRUCTURE;

ALANINE RACEMASE; BACTERIAL PROTEIN; PEPTIDE FRAGMENT; PYRIDOXAL 5 PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; DIMERIZATION; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; GEOBACILLUS STEAROTHERMOPHILUS; MYCOBACTERIUM TUBERCULOSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PSEUDOMONAS AERUGINOSA; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ELECTRON; ENZYMOLOGY; HYDROGEN BOND; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ACTINOBACTERIA (CLASS); GEOBACILLUS STEAROTHERMOPHILUS; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; UNCULTURED ACTINOMYCETE;

ALANINE RACEMASE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CONSERVED SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ELECTRONS; HYDROGEN BONDING; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, TERTIARY; PYRIDOXAL PHOSPHATE;

EID: 13444274582     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0486583     Document Type: Article

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