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Difference between revisions of "User:Wei Peng"
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Wei Peng obtained his Ph.D. at Tsinghua University (Beijing, China) with Prof. Yigong Shi and Prof. Nieng Yan. He was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. Currently as a postdoctoral scholar with Prof. Kim Orth at UT Southwestern Medical Center (Dallas, USA), he has been focusing on host-pathogen interactions. | Wei Peng obtained his Ph.D. at Tsinghua University (Beijing, China) with Prof. Yigong Shi and Prof. Nieng Yan. He was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. Currently as a postdoctoral scholar with Prof. Kim Orth at UT Southwestern Medical Center (Dallas, USA), he has been focusing on host-pathogen interactions. | ||
| − | Wei and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase | + | Wei and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB has a fold called |
| + | Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells. '''AvrB is the founding member of glycosyltransferases with Fido fold''' ([[GT138]]). | ||
Wei contributed to studies on: | Wei contributed to studies on: | ||
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<biblio> | <biblio> | ||
#Peng2024 pmid=38354245 | #Peng2024 pmid=38354245 | ||
| + | #Kinch2009 pmid=19503829 | ||
</biblio> | </biblio> | ||
Revision as of 14:48, 3 January 2025
Wei Peng obtained his Ph.D. at Tsinghua University (Beijing, China) with Prof. Yigong Shi and Prof. Nieng Yan. He was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. Currently as a postdoctoral scholar with Prof. Kim Orth at UT Southwestern Medical Center (Dallas, USA), he has been focusing on host-pathogen interactions.
Wei and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase [1]. AvrB has a fold called Fido [2]. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells. AvrB is the founding member of glycosyltransferases with Fido fold (GT138).
Wei contributed to studies on:
- Peng W, Garcia N, Servage KA, Kohler JJ, Ready JM, Tomchick DR, Fernandez J, and Orth K. (2024). Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4. Sci Adv. 2024;10(7):eadd5108. DOI:10.1126/sciadv.add5108 |
- Kinch LN, Yarbrough ML, Orth K, and Grishin NV. (2009). Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS One. 2009;4(6):e5818. DOI:10.1371/journal.pone.0005818 |