Site-specific protein modifications through pyrroline-carboxy-lysine residues

Autor: Jan Grünewald, Qian Fan, David H. Jones, Ansgar Brock, Linda Okach, Scott A. Lesley, Tiffany Crossgrove, Lisa Quinn, Weijia Ou, Hsien-Po Chiu, Tetsuo Uno, Susan E. Cellitti, Bernhard H. Geierstanger, Paula Patterson, Xueshi Hao

Publikováno v: Proceedings of the National Academy of Sciences. 108:10437-10442

Pyrroline-carboxy-lysine (Pcl) is a demethylated form of pyrrolysine that is generated by the pyrrolysine biosynthetic enzymes when the growth media is supplemented with D-ornithine . Pcl is readily incorporated by the unmodified pyrrolysyl-tRNA/tRNA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01ae8f126a25b2c8d6300ff5801c6d8c
https://doi.org/10.1073/pnas.1105197108

Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules

Autor: Mark W. Knuth, Linda Okach, Keith O. Hodgson, Winnie W Lam, Tamara Astakhova, Debanu Das, Lukasz Jaroszewski, Kevin K. Jin, Abhinav Kumar, Scott A. Lesley, Joanna C Grant, Daniel McMullan, Gye Won Han, Herbert L. Axelrod, Amanda Nopakun, Kyle Ellrott, John Wooley, Piotr Kozbial, Henry J Tien, Polat Abdubek, Christine B Trame, Ashley M. Deacon, Sanjay Krishna, Christopher L. Rife, Henry van den Bedem, Ron Reyes, Lian Duan, Dana Weekes, Adam Godzik, Heath E. Klock, Marc André Elsliger, Carol L. Farr, David Marciano, Ian A. Wilson, Julie Feuerhelm, Christina Puckett, Edward Nigoghossian, Marc C. Deller, Qingping Xu, Constantina Bakolitsa, Connie Chen, Dennis Carlton, Hsiu-Ju Chiu, Mitchell D. Miller, Anna Grzechnik, Thomas Clayton, Andrew T. Morse

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta Crystallographica Section F: Structural Biology and Crystallization Communications

The crystal structure of BT_3984, a SusD-family protein, reveals a TPR N-terminal region providing support for a loop-rich C-terminal subdomain and suggests possible interfaces involved in sus complex formation.
The crystal structure of the Bact

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::651fbda37dbad2454e03450209b718f0
https://doi.org/10.1107/s1744309110032999

Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved α+β core domain and an auxiliary C-terminal treble-clef zinc finger

Autor: Lukasz Jaroszewski, Polat Abdubek, Sanjay Krishna, Adam Godzik, Henry van den Bedem, Dennis Carlton, Marc-André Elsliger, Natasha Sefcovic, Edward Nigoghossian, Piotr Kozbial, Henry J Tien, Thomas Clayton, Debanu Das, Qingping Xu, Joanna C Grant, Gye Won Han, Heath E. Klock, Carol L. Farr, Ron Reyes, Daniel McMullan, John Wooley, Hsiu-Ju Chiu, Marc C. Deller, Herbert L. Axelrod, Connie Chen, Amanda Nopakun, Tamara Astakhova, Ian A. Wilson, Kevin K. Jin, Christine B Trame, Christina Puckett, Constantina Bakolitsa, David Marciano, Keith O. Hodgson, Winnie W Lam, Ashley M. Deacon, Andrew T. Morse, Mitchell D. Miller, Anna Grzechnik, Julie Feuerhelm, Abhinav Kumar, Tiffany Wooten, Dana Weekes, Lian Duan, Linda Okach, Mark W. Knuth, Scott A. Lesley, Kyle Ellrott

Publikováno v: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10

The first structures from the FmdE Pfam family (PF02663) reveal that some members of this family form tightly intertwined dimers consisting of two domains (N-terminal α+β core and C-terminal zinc-finger domains), whereas others contain only the cor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07744ab9a1701e66d2df720abda9b926
http://europepmc.org/articles/PMC2954224

Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiontBacteroides thetaiotaomicron

Autor: Keith O. Hodgson, Kyle Ellrott, Debanu Das, Qingping Xu, Tamara Astakhova, Winnie W Lam, Polat Abdubek, Sanjay Krishna, Mark W. Knuth, Hsiu-Ju Chiu, Andrew Yeh, Jiadong Zhou, Henry van den Bedem, Lukasz Jaroszewski, Thomas Clayton, Linda Okach, Mitchell D. Miller, Anna Grzechnik, Dennis Carlton, Gye Won Han, Heath E. Klock, Abhinav Kumar, Kevin K. Jin, Edward Nigoghossian, Adam Godzik, Christine B Trame, Carol L. Farr, Andrew T. Morse, Dana Weekes, Ron Reyes, Marc C. Deller, Joanna C Grant, Scott A. Lesley, Herbert L. Axelrod, Xiaohui Cai, Piotr Kozbial, Henry J Tien, David Marciano, John Wooley, Tiffany Wooten, Lian Duan, Constantina Bakolitsa, Marc André Elsliger, Connie Chen, Julie Feuerhelm, Ashley M. Deacon, Ian A. Wilson, Christina Puckett, Amanda Nopakun

Publikováno v: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10

The crystal structure of a novel MACPF protein, which may play a role in the adaptation of commensal bacteria to host environments in the human gut, was determined and analyzed.
Membrane-attack complex/perforin (MACPF) proteins are transmembrane

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f11bcb2775a136271482caf7a643ed33
https://doi.org/10.1107/s1744309110023055

Crystal Structure of the First Eubacterial Mre11 Nuclease Reveals Novel Features that May Discriminate Substrates During DNA Repair

Autor: Mitchell D. Miller, Anna Grzechnik, Heath E. Klock, Keith O. Hodgson, Linda Okach, Prasad Burra, Polat Abdubek, John Wooley, Debanu Das, Qingping Xu, Sanjay Krishna, Thomas Clayton, Abhinav Kumar, Henry van den Bedem, Ian A. Wilson, Gye Won Han, Dana Weekes, Davide Moiani, Lian Duan, Christopher L. Rife, Jessica Paulsen, Julie Feuerhelm, Tamara Astakhova, Mark W. Knuth, Marc C. Deller, Ashley M. Deacon, Marc André Elsliger, Scott A. Lesley, Slawomir K. Grzechnik, John A. Tainer, Andrew T. Morse, Daniel McMullan, Lukasz Jaroszewski, Dennis Carlton, Edward Nigoghossian, Christine B Trame, David Marciano, Herbert L. Axelrod, Natasha Sefcovic, Hsiu-Ju Chiu, Joanna C Grant, Adam Godzik, Ron Reyes, Piotr Kozbial, Henry J Tien, Kevin K. Jin, Dustin C. Ernst

Publikováno v: Journal of Molecular Biology. 397:647-663

Mre11 nuclease plays a central role in the repair of cytotoxic and mutagenic DNA double-strand breaks. As X-ray structural information has been available only for the Pyrococcus furiosus enzyme (PfMre11), the conserved and variable features of this n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc6eaa2eb616c362f7a1e7a65e393b70
https://doi.org/10.1016/j.jmb.2010.01.049