The 0.83 Å resolution crystal structure of α-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain

Journal of Molecular Biology

Volumn 338, Issue 5, 2004, Pages 999-1013

  Fuhrmann, Cynthia N ^a   Kelch, Brian A ^a   Ota, Nobuyuki ^a   Agard, David A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Atomic resolution crystallography; Packing distortion; Protein folding; Serine protease catalysis; SGPB, Streptomyces griseus protease B; SGPE, Streptomyces griseus protease E; lytic protease; LP, lytic protease

Indexed keywords

ASPARTIC ACID; CARBON; CHYMOTRYPSIN; HISTIDINE; HYDROGEN; PHENYLALANINE; PROTEINASE; SERINE PROTEINASE; SULFATE; THREONINE; MYXOBACTER ALPHA LYTIC PROTEINASE; MYXOBACTER ALPHA-LYTIC PROTEINASE;

ARTICLE; CALCULATION; CATALYSIS; CRYSTAL STRUCTURE; ENVIRONMENTAL FACTOR; GEOMETRY; HYDROGEN BOND; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT; STATISTICAL SIGNIFICANCE; STEREOSPECIFICITY; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); STREPTOMYCES; STREPTOMYCES GRISEUS;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES; SULFATES;

EID: 2142715907     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.018     Document Type: Article

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