Structural studies of the YedU stress protein

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Structural studies of the YedU stress protein

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dc.contributor.advisor Robert O. Fox en_US
dc.creator Yonghong Zhao en_US
dc.date.accessioned 2011-12-20T16:05:26Z
dc.date.available 2005-09-15 en_US
dc.date.available 2011-12-20T16:05:26Z
dc.date.created 2004-10-28 en_US
dc.date.issued 2004-11-12 en_US
dc.identifier.other etd-10282004-152543 en_US
dc.identifier.uri http://hdl.handle.net/2152.3/242
dc.description.abstract The knowledge of stress proteins is important for understanding stress response, pathology of a broad set of diseases, and the development of therapeutics. The Escherichia coli YedU stress protein, also known as Hsp31, is highly induced upon heat shock. To obtain a better understanding for the possible molecular function of the YedU stress protein, it was expressed, purified, and crystallized. The crystal structure of YedU was determined at 2.2 Å resolution in a multiple isomorphous replacement (MIR) experiment. \r\nYedU monomer has an alpha/beta/alpha sandwich domain and a second smaller domain. Between the sandwich domain and the second smaller domain, there is a putative catalytic triad composed of Cys184, His185, and Asp213. A metal-binding site was identified, where a zinc(II) ion is coordinated by a 2-His-1-carboxylate motif composed of His85, Glu90, and His122. The possible functions of the metal-binding site and the Cys184-His185-Asp213 triad are discussed. \r\nIt was reported that YedU has chaperone activity in vitro. YedU forms dimers in solution and the dimer interface was identified. The molecular surface of the YedU homodimer exhibits a number of solvent-exposed hydrophobic patches that are reminiscent of substrate-binding sites of molecular chaperones. To investigate the role of a central hydrophobic patch in substrate binding, four mutants were made, each replacing a hydrophobic residue with a charged residue. Compared with the wild type YedU protein, the chaperone activity of these mutants was only slightly reduced, suggesting that these residues alone do not play a dominant role in substrate binding at high temperatures. en_US
dc.format.medium electronic en_US
dc.language.iso eng en_US
dc.rights Copyright © is held by the author. Presentation of this material on the TDL web site by The University of Texas Medical Branch at Galveston was made possible under a limited license grant from the author who has retained all copyrights in the works. en_US
dc.subject X-ray crystallography en_US
dc.subject protease en_US
dc.subject metalloprotein en_US
dc.title Structural studies of the YedU stress protein en_US
dc.type.material text en_US
dc.type.genre dissertation en_US
thesis.degree.name PhD en_US
thesis.degree.level Doctoral en_US
thesis.degree.grantor The University of Texas Medical Branch en_US
thesis.degree.department Cellular Physiology and Molecular Biophysics en_US
dc.contributor.committeeMember Vincent J. Hilser en_US
dc.contributor.committeeMember Luis Reuss en_US
dc.contributor.committeeMember Hiram F. Gilbert en_US
dc.contributor.committeeMember David W. Bolen en_US

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