Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA - Implications for the catalytic mechanism of parvulins

BMC Structural Biology

Volumn 9, Issue , 2009, Pages

  Heikkinen, Outi ^a   Seppala, Raili ^b   Tossavainen, Helena ^b   Heikkinen, Sami ^a   Koskela, Harri ^a   Permi, Perttu ^b   Kilpeläinen, Ilkka ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; LIPOPROTEIN; PARVULIN; PEPTIDYLPROLYL ISOMERASE; PRSA PROTEIN; UNCLASSIFIED DRUG; ENZYME INHIBITOR; NIMA INTERACTING PEPTIDYLPROLYL ISOMERASE; NIMA-INTERACTING PEPTIDYLPROLYL ISOMERASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME SUBSTRATE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEIN TARGETING; STAPHYLOCOCCUS AUREUS; TITRIMETRY; BIOSYNTHESIS; CHEMISTRY; ENZYMOLOGY; ISOLATION AND PURIFICATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE;

BACTERIA (MICROORGANISMS); POSIBACTERIA; STAPHYLOCOCCUS AUREUS;

CATALYTIC DOMAIN; ENZYME INHIBITORS; HISTIDINE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDYLPROLYL ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; STAPHYLOCOCCUS AUREUS;

EID: 66149149408     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-9-17     Document Type: Article

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