Structural basis for Zn2+-dependent intercellular adhesion in staphylococcal biofilms

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 3, 2013, Pages

  Conrady, Deborah G ^a,b   Wilson, Jeffrey J ^a   Herr, Andrew B ^a  

^a UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

G5 domain; Self assembly; Staphylococci; X ray crystallography; Zinc

Indexed keywords

BACTERIAL PROTEIN; DIMER; SOLVENT; ZINC ION; BACTERIAL DNA; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; SASG PROTEIN, STAPHYLOCOCCUS AUREUS; ZINC;

AMINO ACID ANALYSIS; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL CELL; BETA SHEET; BIOFILM; CELL ADHESION; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ENVIRONMENTAL FACTOR; HYDROPHILICITY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIUM ADHERENCE; BINDING SITE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; GROWTH, DEVELOPMENT AND AGING; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PATHOGENICITY; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STAPHYLOCOCCUS; STATIC ELECTRICITY; X RAY CRYSTALLOGRAPHY;

STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL ADHESION; BACTERIAL PROTEINS; BASE SEQUENCE; BINDING SITES; BIOFILMS; CRYSTALLOGRAPHY, X-RAY; DNA, BACTERIAL; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; REPETITIVE SEQUENCES, AMINO ACID; SEQUENCE HOMOLOGY, AMINO ACID; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS; STATIC ELECTRICITY; ZINC;

MLCS; MLOWN;

EID: 84872553494     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1208134110     Document Type: Article

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