Structural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen staphylococcus saprophyticus

Proteins: Structure, Function and Bioinformatics

Volumn 74, Issue 2, 2009, Pages 515-519

  Rossi, Paolo ^a,b   Aramini, James M ^a,b   Xiao, Rong ^a,b   Chen, Chen X ^a,b   Nwosu, Chioma ^a,b   Owens, Leah A ^a,b   Maglaqui, Melissa ^a,b   Nair, Rajesh ^b,c   Fischer, Markus ^b,c   Acton, Thomas B ^a,b   Honig, Barry ^b,c   Rost, Burkhard ^b,c   Montelione, Gaetano T ^a,b,d  

^a RUTGERS UNIVERSITY   (United States)

^b RUTGERS UNIVERSITY   (United States)

^c Och Spine at New York Presbyterian Hospitals   (United States)

^d RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

Chap domain; Endopeptidase; Nmr structure; Secretory antigen

Indexed keywords

BACTERIAL ANTIGEN; BACTERIAL ENZYME; CARBON 13; CHAP DOMAIN ENZYME; CYSTEINE HISTIDINE DEPENDENT AMIDOHYDROLASE PEPTIDASE; CYSTEINE PEPTIDASE; NITROGEN 15; PROTEINASE; SECRETORY ANTIGEN; UNCLASSIFIED DRUG; ASPARAGINE; BACTERIAL PROTEIN; CYSTEINE; GLUTAMIC ACID; HISTIDINE;

ARTICLE; BACTERIAL VIRULENCE; ENZYME STRUCTURE; GRAM POSITIVE BACTERIUM; MOLECULAR DYNAMICS; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STAPHYLOCOCCUS SAPROPHYTICUS; STRUCTURE ANALYSIS; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN TERTIARY STRUCTURE; STAPHYLOCOCCUS;

STAPHYLOCOCCUS SAPROPHYTICUS;

ASPARAGINE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CYSTEINE; ENDOPEPTIDASES; GLUTAMIC ACID; HISTIDINE; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN STRUCTURE, TERTIARY; STAPHYLOCOCCUS;

EID: 59449109206     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22267     Document Type: Article

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