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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]]
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Wei Peng obtained his Ph.D. at Tsinghua University in China with Prof. Yigong Shi and Prof. Nieng Yan, where he was trained as a structural biologist using protein crystallography or cryo-EM and other tools to investigate protein functions. As a postdoc with Prof. Kim Orth at UT Southwestern Medical Center, he has discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase (with a fold called Fido) that catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate<cite>Peng2024</cite>.
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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.  
  
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* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.
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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]]).
  
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Wei contributed to studies on:
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* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite>
  
  

Latest revision as of 15:02, 18 December 2024

Wei-Peng.jpeg

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:

  • GT138 Pseudomonas syringae rhamnosyltransferase AvrB [1]


  1. 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 | PubMed ID:38354245 [Peng2024]
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