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Difference between revisions of "User:Wei Peng"
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[[Image:Wei-Peng.jpeg|200px|right]] | [[Image:Wei-Peng.jpeg|200px|right]] | ||
| − | Wei Peng obtained his Ph.D. at Tsinghua University | + | 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 (with a fold called Fido) <cite>Peng2024</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 and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase (with a fold called Fido) <cite>Peng2024</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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* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite> | * [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite> | ||
Latest revision as of 15:02, 18 December 2024
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 (with a fold called Fido) [1]. 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: