Affiliation: Harvard University
- Structure of a bacterial homologue of vitamin K epoxide reductaseWeikai Li
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Nature 463:507-12. 2010..Our results have implications for the mechanism of the mammalian VKOR and explain how mutations can cause resistance to the VKOR inhibitor warfarin, the most commonly used oral anticoagulant...
- The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane sealWeikai Li
Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA
Mol Cell 26:511-21. 2007..Our data show that the plug domain is required to maintain a closed state of the channel and suggest a mechanism for channel gating...
- Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partnersSol Schulman
Department of Cell Biology, Harvard Medical School, Howard Hughes Medical Institute, 240 Longwood Avenue, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 107:15027-32. 2010..Taken together, our results demonstrate that human VKOR employs the same electron transfer pathway as its bacterial homologs and that VKORs generally prefer membrane-bound Trx-like redox partners...
- Crystal structure of an unusual thioredoxin protein with a zinc finger domainJiqing Ye
Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
J Biol Chem 282:34945-51. 2007..On the basis of structural similarity to the zinc fingers in Npl4 and Vps36, we propose that the N-terminal zinc finger of thioredoxin-2 mediates protein-protein interactions, possibly with its substrates or chaperones...
- A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecAJochen Zimmer
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA
J Mol Biol 364:259-65. 2006..subtilis SecA suggests that small changes in the nucleotide binding domains could be amplified via helix 1 of the helical scaffold domain (hsd) to generate larger movements of the domains involved in polypeptide binding...