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Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism

The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+β fold comprising two β-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokary...

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Autores principales: Bakolitsa, Constantina, Kumar, Abhinav, Carlton, Dennis, Miller, Mitchell D., Krishna, S. Sri, Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L., Chiu, Hsiu-Ju, Clayton, Thomas, Deller, Marc C., Duan, Lian, Elsliger, Marc-André, Feuerhelm, Julie, Grzechnik, Slawomir K., Grant, Joanna C., Han, Gye Won, Jaroszewski, Lukasz, Jin, Kevin K., Klock, Heath E., Knuth, Mark W., Kozbial, Piotr, Marciano, David, McMullan, Daniel, Morse, Andrew T., Nigoghossian, Edward, Okach, Linda, Oommachen, Silvya, Paulsen, Jessica, Reyes, Ron, Rife, Christopher L., Tien, Henry J., Trout, Christina V., van den Bedem, Henry, Weekes, Dana, Xu, Qingping, Hodgson, Keith O., Wooley, John, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., Wilson, Ian A.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954206/
https://www.ncbi.nlm.nih.gov/pubmed/20944212
http://dx.doi.org/10.1107/S1744309109023689
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author Bakolitsa, Constantina
Kumar, Abhinav
Carlton, Dennis
Miller, Mitchell D.
Krishna, S. Sri
Abdubek, Polat
Astakhova, Tamara
Axelrod, Herbert L.
Chiu, Hsiu-Ju
Clayton, Thomas
Deller, Marc C.
Duan, Lian
Elsliger, Marc-André
Feuerhelm, Julie
Grzechnik, Slawomir K.
Grant, Joanna C.
Han, Gye Won
Jaroszewski, Lukasz
Jin, Kevin K.
Klock, Heath E.
Knuth, Mark W.
Kozbial, Piotr
Marciano, David
McMullan, Daniel
Morse, Andrew T.
Nigoghossian, Edward
Okach, Linda
Oommachen, Silvya
Paulsen, Jessica
Reyes, Ron
Rife, Christopher L.
Tien, Henry J.
Trout, Christina V.
van den Bedem, Henry
Weekes, Dana
Xu, Qingping
Hodgson, Keith O.
Wooley, John
Deacon, Ashley M.
Godzik, Adam
Lesley, Scott A.
Wilson, Ian A.
author_facet Bakolitsa, Constantina
Kumar, Abhinav
Carlton, Dennis
Miller, Mitchell D.
Krishna, S. Sri
Abdubek, Polat
Astakhova, Tamara
Axelrod, Herbert L.
Chiu, Hsiu-Ju
Clayton, Thomas
Deller, Marc C.
Duan, Lian
Elsliger, Marc-André
Feuerhelm, Julie
Grzechnik, Slawomir K.
Grant, Joanna C.
Han, Gye Won
Jaroszewski, Lukasz
Jin, Kevin K.
Klock, Heath E.
Knuth, Mark W.
Kozbial, Piotr
Marciano, David
McMullan, Daniel
Morse, Andrew T.
Nigoghossian, Edward
Okach, Linda
Oommachen, Silvya
Paulsen, Jessica
Reyes, Ron
Rife, Christopher L.
Tien, Henry J.
Trout, Christina V.
van den Bedem, Henry
Weekes, Dana
Xu, Qingping
Hodgson, Keith O.
Wooley, John
Deacon, Ashley M.
Godzik, Adam
Lesley, Scott A.
Wilson, Ian A.
author_sort Bakolitsa, Constantina
collection PubMed
description The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+β fold comprising two β-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokaryotic S-adenosylmethionine decarboxylases, is consistent with a role in amino-acid metabolism. Genomic neighborhood analysis of LP2179 supports this functional assignment, which might also then be extended to PF08868 and PF08968.
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spelling pubmed-29542062010-10-27 Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism Bakolitsa, Constantina Kumar, Abhinav Carlton, Dennis Miller, Mitchell D. Krishna, S. Sri Abdubek, Polat Astakhova, Tamara Axelrod, Herbert L. Chiu, Hsiu-Ju Clayton, Thomas Deller, Marc C. Duan, Lian Elsliger, Marc-André Feuerhelm, Julie Grzechnik, Slawomir K. Grant, Joanna C. Han, Gye Won Jaroszewski, Lukasz Jin, Kevin K. Klock, Heath E. Knuth, Mark W. Kozbial, Piotr Marciano, David McMullan, Daniel Morse, Andrew T. Nigoghossian, Edward Okach, Linda Oommachen, Silvya Paulsen, Jessica Reyes, Ron Rife, Christopher L. Tien, Henry J. Trout, Christina V. van den Bedem, Henry Weekes, Dana Xu, Qingping Hodgson, Keith O. Wooley, John Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. Acta Crystallogr Sect F Struct Biol Cryst Commun New Folds The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+β fold comprising two β-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokaryotic S-adenosylmethionine decarboxylases, is consistent with a role in amino-acid metabolism. Genomic neighborhood analysis of LP2179 supports this functional assignment, which might also then be extended to PF08868 and PF08968. International Union of Crystallography 2009-10-27 /pmc/articles/PMC2954206/ /pubmed/20944212 http://dx.doi.org/10.1107/S1744309109023689 Text en © Bakolitsa et al. 2010 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle New Folds
Bakolitsa, Constantina
Kumar, Abhinav
Carlton, Dennis
Miller, Mitchell D.
Krishna, S. Sri
Abdubek, Polat
Astakhova, Tamara
Axelrod, Herbert L.
Chiu, Hsiu-Ju
Clayton, Thomas
Deller, Marc C.
Duan, Lian
Elsliger, Marc-André
Feuerhelm, Julie
Grzechnik, Slawomir K.
Grant, Joanna C.
Han, Gye Won
Jaroszewski, Lukasz
Jin, Kevin K.
Klock, Heath E.
Knuth, Mark W.
Kozbial, Piotr
Marciano, David
McMullan, Daniel
Morse, Andrew T.
Nigoghossian, Edward
Okach, Linda
Oommachen, Silvya
Paulsen, Jessica
Reyes, Ron
Rife, Christopher L.
Tien, Henry J.
Trout, Christina V.
van den Bedem, Henry
Weekes, Dana
Xu, Qingping
Hodgson, Keith O.
Wooley, John
Deacon, Ashley M.
Godzik, Adam
Lesley, Scott A.
Wilson, Ian A.
Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
title Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
title_full Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
title_fullStr Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
title_full_unstemmed Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
title_short Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
title_sort structure of lp2179, the first representative of pfam family pf08866, suggests a new fold with a role in amino-acid metabolism
topic New Folds
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954206/
https://www.ncbi.nlm.nih.gov/pubmed/20944212
http://dx.doi.org/10.1107/S1744309109023689
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