The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity

Protein Science

Volumn 19, Issue 1, 2010, Pages 6-18

  Weininger, Ulrich ^a   Jakob, Roman P ^b   Kovermann, Michael ^a   Balbach, Jochen ^a   Schmid, Franz X ^b  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Parvulin; Periplasm; Pin1; Prolyl isomerase; Protein maturation; SecYEG; SurA

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PARVULIN; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE D; PROTEIN SURA; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ARTICLE; BACILLUS SUBTILIS; BINDING SITE; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; ISOMERIZATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STAPHYLOCOCCUS AUREUS;

ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDYLPROLYL ISOMERASE; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

EID: 75149136165     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.277     Document Type: Article

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