Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 Å resolution

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

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 75:264-271

The protein SO4266 (gi|24375750) from the bacterium Shewanella oneidensis MR-1 is annotated as a member of Pfam PF02661. This family consists of Fic (filamentation induced by cAMP) proteins and their relatives, and is characterized by the presence of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe4426ccda2864402a2136f6120bc09b
https://doi.org/10.1002/prot.22338

Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA

Autor: Chloe Zubieta, Abhinav Kumar, Keith O. Hodgson, Aprilfawn White, Mark W. Knuth, Polat Abdubek, Rosanne Joseph, Marc C. Deller, David Marciano, Heath E. Klock, Sanjay Krishna, Lian Duan, Hsiu-Ju Chiu, Slawomir K. Grzechnik, Scott A. Lesley, Henry van den Bedem, Paul Schimmel, Linda Okach, Gye Won Han, Silvya Oommachen, John Wooley, Christopher L. Rife, Mitchell D. Miller, Claire Acosta, Marc-André Elsliger, Edward Nigoghossian, Daniel McMullan, Mili Kapoor, Dana Weekes, Herbert L. Axelrod, Ylva Elias, Dennis Carlton, Lukasz Jaroszewski, Thomas Clayton, Tamara Astakhova, Julie Feuerhelm, Christina V. Trout, Kevin K. Jin, Joanna Hale, Qingping Xu, Ashley M. Deacon, Ian A. Wilson, Andrew T. Morse, Kevin D. Murphy, Adam Godzik, Piotr Kozbial, Ron Reyes

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 69:234-243

TyrA is a member of the dye-decolorizing peroxidase (DyP) family, a new family of heme-dependent peroxidase recently identified in fungi and bacteria. Here, we report the crystal structure of TyrA in complex with iron protoporphyrin (IX) at 2.3 A. Ty

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbf6af72a83fca6a8e2f3803f5061878
https://doi.org/10.1002/prot.21673

Conformational changes associated with the binding of zinc acetate at the putative active site of XcTcmJ, a cupin from Xanthomonas campestris pv. campestris

Autor: Kevin D. Murphy, Ian A. Wilson, Adam Godzik, Jonathan M. Caruthers, Kevin K. Jin, Marc-André Elsliger, Linda Okach, Edward Nigoghossian, Scott A. Lesley, John Wooley, Claire Acosta, Chloe Zubieta, Lukasz Jaroszewski, Aprilfawn White, Ron Reyes, Slawomir K. Grzechnik, Marc C. Deller, Mark W. Knuth, Ashley M. Deacon, David Marciano, Lian Duan, Qingping Xu, Christopher L. Rife, Hsiu-Ju Chiu, Piotr Kozbial, Abhinav Kumar, Henry J Tien, Julie Feuerhelm, Joanna C Grant, Jessica Paulsen, Dennis Carlton, Mitchell D. Miller, Dana Weekes, Daniel McMullan, Tamara Astakhova, Thomas Clayton, Christina V. Trout, Polat Abdubek, Ylva Elias, Sanjay Krishna, Andrew T. Morse, Heath E. Klock, Herbert L. Axelrod, Gye Won Han, Keith O. Hodgson, Silvya Oommachen, Henry van den Bedem

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 an RmlC-type cupin with zinc acetate bound at the putative active site reveals significant differences from a previous structure without any bound ligand. The functional implications of the ligand-induced conformational chang

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65d7af94ee485f11baa3bd5c5de4674e
https://escholarship.org/uc/item/3bz276fw

Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism

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

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

Structures of the first representatives of PF06684 (DUF1185) reveal a Bacillus chorismate mutase-like fold with a potential role in amino-acid synthesis.
The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d261a4239ffea9fcc0956dd9c1a34aae
https://escholarship.org/uc/item/5pr2282m

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

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

Publikováno v: Proteins. 75(2)

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 similari

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c089b20072de60553e2f07ff580b4b3c
https://pubmed.ncbi.nlm.nih.gov/19173316