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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 10(66), p. 1230-1236, 2009

DOI: 10.1107/s1744309109022192

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Structure of an essential bacterial protein YeaZ (TM0874) fromThermotoga maritimaat 2.5 Å resolution

Journal article published in 2009 by Qingping Xu, Daniel McMullan, Lukasz Jaroszewski, S. Sri Krishna, Marc-André Elsliger, Andrew P. Yeh, Polat Abdubek, Tamara Astakhova, Herbert L. Axelrod, Dennis Carlton, Hsiu-Ju Chiu, Thomas Clayton, Lian Duan, Julie Feuerhelm, Joanna Grant and other authors.
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.