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Volumn 20, Issue 18, 2001, Pages 5033-5039
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Crystal structure of the outer membrane protease Ompt from Escherichia coli suggests a novel catalytic site
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Author keywords
His Asp dyad; Lipopolysaccharide; OmpT; Omptin; Protease
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Indexed keywords
ASPARTIC ACID;
HISTIDINE;
LIPOPOLYSACCHARIDE;
PROTEINASE;
ARTICLE;
BINDING SITE;
CATALYSIS;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ESCHERICHIA COLI;
EXTRACELLULAR SPACE;
GRAM NEGATIVE BACTERIUM;
LIPID BILAYER;
OUTER MEMBRANE;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
VIRULENCE;
AMINO ACID SEQUENCE;
ASPARTIC ACID;
BINDING SITES;
CATALYTIC DOMAIN;
CRYSTALLOGRAPHY, X-RAY;
ESCHERICHIA COLI;
HISTIDINE;
LIPOPOLYSACCHARIDES;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
SERINE ENDOPEPTIDASES;
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EID: 0035903650
PISSN: 02614189
EISSN: None
Source Type: Journal
DOI: 10.1093/emboj/20.18.5033 Document Type: Article |
Times cited : (222)
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References (38)
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