Crystal Structure Determination and Functional Characterization of the Metallochaperone SlyD from Thermus thermophilus-Reference-Cited by-同舟云学术

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Crystal Structure Determination and Functional Characterization of the Metallochaperone SlyD from Thermus thermophilus

Published:2010-05 Issue:3 Volume:398 Page:375-390
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Löw Christian,Neumann Piotr,Tidow Henning,Weininger Ulrich,Haupt Caroline,Friedrich-Epler Beatrice,Scholz Christian,Stubbs Milton T.,Balbach Jochen

Funder

Deutsche Forschungsgemeinschaft

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference79 articles.

1. slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis–trans-isomerases;Roof;J. Biol. Chem.,1994

2. The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase;Hottenrott;J. Biol. Chem.,1997

3. Peptidylproline cis/trans isomerases;Galat;Prog. Biophys. Mol. Biol.,1995

4. Catalysis of proline-directed protein phosphorylation by peptidyl-prolyl cis/trans isomerases;Weiwad;J. Mol. Biol.,2004

5. DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone;Graubner;J. Biol. Chem.,2007

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