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Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution

YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks...

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Autores principales: Xu, Qingping, McMullan, Daniel, Jaroszewski, Lukasz, Krishna, S. Sri, Elsliger, Marc-André, Yeh, Andrew P., Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L., Carlton, Dennis, Chiu, Hsiu-Ju, Clayton, Thomas, Duan, Lian, Feuerhelm, Julie, Grant, Joanna, Han, Gye Won, Jin, Kevin K., Klock, Heath E., Knuth, Mark W., Miller, Mitchell D., Morse, Andrew T., Nigoghossian, Edward, Okach, Linda, Oommachen, Silvya, Paulsen, Jessica, Reyes, Ron, Rife, Christopher L., van den Bedem, Henry, 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/PMC2954210/
https://www.ncbi.nlm.nih.gov/pubmed/20944216
http://dx.doi.org/10.1107/S1744309109022192
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author Xu, Qingping
McMullan, Daniel
Jaroszewski, Lukasz
Krishna, S. Sri
Elsliger, Marc-André
Yeh, Andrew P.
Abdubek, Polat
Astakhova, Tamara
Axelrod, Herbert L.
Carlton, Dennis
Chiu, Hsiu-Ju
Clayton, Thomas
Duan, Lian
Feuerhelm, Julie
Grant, Joanna
Han, Gye Won
Jin, Kevin K.
Klock, Heath E.
Knuth, Mark W.
Miller, Mitchell D.
Morse, Andrew T.
Nigoghossian, Edward
Okach, Linda
Oommachen, Silvya
Paulsen, Jessica
Reyes, Ron
Rife, Christopher L.
van den Bedem, Henry
Hodgson, Keith O.
Wooley, John
Deacon, Ashley M.
Godzik, Adam
Lesley, Scott A.
Wilson, Ian A.
author_facet Xu, Qingping
McMullan, Daniel
Jaroszewski, Lukasz
Krishna, S. Sri
Elsliger, Marc-André
Yeh, Andrew P.
Abdubek, Polat
Astakhova, Tamara
Axelrod, Herbert L.
Carlton, Dennis
Chiu, Hsiu-Ju
Clayton, Thomas
Duan, Lian
Feuerhelm, Julie
Grant, Joanna
Han, Gye Won
Jin, Kevin K.
Klock, Heath E.
Knuth, Mark W.
Miller, Mitchell D.
Morse, Andrew T.
Nigoghossian, Edward
Okach, Linda
Oommachen, Silvya
Paulsen, Jessica
Reyes, Ron
Rife, Christopher L.
van den Bedem, Henry
Hodgson, Keith O.
Wooley, John
Deacon, Ashley M.
Godzik, Adam
Lesley, Scott A.
Wilson, Ian A.
author_sort Xu, Qingping
collection PubMed
description YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes.
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spelling pubmed-29542102010-10-27 Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution Xu, Qingping McMullan, Daniel Jaroszewski, Lukasz Krishna, S. Sri Elsliger, Marc-André Yeh, Andrew P. Abdubek, Polat Astakhova, Tamara Axelrod, Herbert L. Carlton, Dennis Chiu, Hsiu-Ju Clayton, Thomas Duan, Lian Feuerhelm, Julie Grant, Joanna Han, Gye Won Jin, Kevin K. Klock, Heath E. Knuth, Mark W. Miller, Mitchell D. Morse, Andrew T. Nigoghossian, Edward Okach, Linda Oommachen, Silvya Paulsen, Jessica Reyes, Ron Rife, Christopher L. van den Bedem, Henry Hodgson, Keith O. Wooley, John Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. Acta Crystallogr Sect F Struct Biol Cryst Commun Novel Variants of Known Folds and Function YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes. International Union of Crystallography 2009-10-27 /pmc/articles/PMC2954210/ /pubmed/20944216 http://dx.doi.org/10.1107/S1744309109022192 Text en © Xu 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 Novel Variants of Known Folds and Function
Xu, Qingping
McMullan, Daniel
Jaroszewski, Lukasz
Krishna, S. Sri
Elsliger, Marc-André
Yeh, Andrew P.
Abdubek, Polat
Astakhova, Tamara
Axelrod, Herbert L.
Carlton, Dennis
Chiu, Hsiu-Ju
Clayton, Thomas
Duan, Lian
Feuerhelm, Julie
Grant, Joanna
Han, Gye Won
Jin, Kevin K.
Klock, Heath E.
Knuth, Mark W.
Miller, Mitchell D.
Morse, Andrew T.
Nigoghossian, Edward
Okach, Linda
Oommachen, Silvya
Paulsen, Jessica
Reyes, Ron
Rife, Christopher L.
van den Bedem, Henry
Hodgson, Keith O.
Wooley, John
Deacon, Ashley M.
Godzik, Adam
Lesley, Scott A.
Wilson, Ian A.
Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution
title Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution
title_full Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution
title_fullStr Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution
title_full_unstemmed Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution
title_short Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution
title_sort structure of an essential bacterial protein yeaz (tm0874) from thermotoga maritima at 2.5 å resolution
topic Novel Variants of Known Folds and Function
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954210/
https://www.ncbi.nlm.nih.gov/pubmed/20944216
http://dx.doi.org/10.1107/S1744309109022192
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