A highly conserved interaction involving the middle residue of the SXN active-site motif is crucial for function of class B penicillin-binding proteins: Mutational and computational analysis of PBP 2 from N. gonorrhoeae

Biochemistry

Volumn 51, Issue 13, 2012, Pages 2775-2784

  Tomberg, Joshua ^a   Temple, Brenda ^a,b   Fedarovich, Alena ^c   Davies, Christopher ^c   Nicholas, Robert A ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

^c MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ASPARTATE RESIDUE; ASPARTATES; CLASS B; COMPUTATIONAL ANALYSIS; GONORRHOEAE; NEISSERIA GONORRHOEAE; PENICILLIN G; PENICILLIN-BINDING PROTEINS;

ACYLATION; AMINO ACIDS; EQUIVALENCE CLASSES;

DRUG PRODUCTS;

ASPARTIC ACID; GAMMA GLUTAMYLTRANSFERASE; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 2; PENICILLIN G; SERINE; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG;

ACYLATION; ANTIBIOTIC SENSITIVITY; ARTICLE; BIOLOGY; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG PROTEIN BINDING; ENZYME ACTIVITY; GENE MUTATION; MOLECULAR INTERACTION; MUTANT; MUTATIONAL ANALYSIS; NEISSERIA GONORRHOEAE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; RESIDUE ANALYSIS;

CATALYTIC DOMAIN; CONSERVED SEQUENCE; MODELS, MOLECULAR; MUTATION; NEISSERIA GONORRHOEAE; PENICILLIN-BINDING PROTEINS;

NEISSERIA GONORRHOEAE;

EID: 84859414020     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2017987     Document Type: Article

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