A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Å resolution

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

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 BT1062 from Bacteroides thetaiotaomicron revealed a conserved fold that is widely adopted by fimbrial components.
BT1062 from Bacteroides thetaiotaomicron is a homolog of Mfa2 (PGN0288 or PG0179), which is a component of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::007ddefbe60d7894f526bbc973ac2fbb
http://europepmc.org/articles/PMC2954217

Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction

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

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 structures of SPO0140 and Sbal_2486 revealed a two-domain structure that adopts a novel fold. Analysis of the interdomain cleft suggests a nucleotide-based ligand with a genome context indicating signaling as a possible role for this fami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07ddc311bafe8a0009c9a53325b96ebf
http://europepmc.org/articles/PMC2954208

The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold

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

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

KPN03535 is a protein unique to K. pneumoniae. The crystal structure reveals that KPN03535 represents a novel variant of the OB-fold and is likely to be a DNA-binding lipoprotein.
KPN03535 (gi|152972051) is a putative lipoprotein of unknown func

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bd09c4d3f24cc38b69b4c4fafc18191
http://europepmc.org/articles/PMC2954213

Crystal structure of a novel Sm-like protein of putative cyanophage origin at 2.60 Å resolution

Autor: Lukasz Jaroszewski, Ashley M. Deacon, Julie Feuerhelm, Hsiu-Ju Chiu, Debanu Das, Dana Weekes, Jessica Paulsen, Qingping Xu, Marc C. Deller, Piotr Kozbial, Ian A. Wilson, Christina Puckett, Gye Won Han, Silvya Oommachen, Abhinav Kumar, Marc André Elsliger, Amanda Nopakun, Natasha Sefcovic, Linda Okach, Edward Nigoghossian, Herbert L. Axelrod, Keith O. Hodgson, Dennis Carlton, Scott A. Lesley, Mark W. Knuth, Heath E. Klock, Henry Tien, Carol L. Farr, Kevin D. Murphy, Hope A. Johnson, Slawomir K. Grzechnik, Kevin K. Jin, Henry van den Bedem, Ylva Elias, Adam Godzik, Dustin C. Ernst, Tamara Astakhova, Andrew T. Morse, Aprilfawn White, Thomas Clayton, John Wooley, Connie Chen, Christine B Trame, Daniel McMullan, Christina V. Trout, Joanna Hale, Ron Reyes, Claire Acosta, David Marciano, Polat Abdubek, Lian Duan, Sanjay Krishna, Christopher L. Rife, Prasad Burra, Sebastian Sudek, Mitchell D. Miller, Anna Grzechnik

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 75:296-307

ECX21941 represents a very large family (over 600 members) of novel, ocean metagenome-specific proteins identified by clustering of the dataset from the Global Ocean Sampling expedition. The crystal structure of ECX21941 reveals unexpected similarity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c4d37954466f96b1dafb5c692f74eb85
https://doi.org/10.1002/prot.22360

MORPH-PRO: a novel algorithm and web server for protein morphing

Autor: Andrey Lushnikov, Natalie Castellana, Pavel A. Pevzner, Natasha Sefcovic, Piotr Rotkiewicz, Kira Vyatkina, Adam Godzik

Publikováno v: Castellana, Natalie E; Lushnikov, Andrey; Rotkiewicz, Piotr; Sefcovic, Natasha; Pevzner, Pavel A; Godzik, Adam; et al.(2013). MORPH-PRO: a novel algorithm and web server for protein morphing. Algorithms for Molecular Biology, 8(1), 19. doi: http://dx.doi.org/10.1186/1748-7188-8-19. Retrieved from: http://www.escholarship.org/uc/item/14g9r9r8
Algorithms for Molecular Biology : AMB

Background Proteins are known to be dynamic in nature, changing from one conformation to another while performing vital cellular tasks. It is important to understand these movements in order to better understand protein function. At the same time, ex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43c01f80a5f5b1a5de7ba7efbf54ce08
http://www.escholarship.org/uc/item/14g9r9r8