Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding

Protein Science

Volumn 15, Issue 4, 2006, Pages 774-784

  Kotaka, Masayo ^a   Dhaliwal, Balvinder ^a   Ren, Jingshan ^a   Nichols, Charles E ^a   Angell, Richard ^b   Lockyer, Michael ^b   Hawkins, Alastair R ^c   Stammers, David K ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b Arrow Therapeutics   (United Kingdom)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

Drug design; S. Aureus; Substrate induced conformational change; Thymidylate kinase; X ray crystallography

Indexed keywords

PHOSPHOTRANSFERASE; PROLINE; THYMIDINE PHOSPHATE; THYMIDYLATE KINASE; THYMINE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DRUG BINDING; DRUG DESIGN; DRUG STRUCTURE; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEOSIDE-PHOSPHATE KINASE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; STAPHYLOCOCCUS AUREUS; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MYCOBACTERIUM TUBERCULOSIS; STAPHYLOCOCCUS AUREUS;

EID: 33645508875     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.052002406     Document Type: Article

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