Structural studies of PMM/PGM from Pseudomonas aeruginosa

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Structural studies of PMM/PGM from Pseudomonas aeruginosa

Please use this identifier to cite or link to this item: http://hdl.handle.net/10355/4134

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dc.contributor.advisor Beamer, Lesa J. (Lesa Jean) en
dc.contributor.author Regni, Catherine A., 1973- en_US
dc.date.accessioned 2010-01-06T21:19:06Z
dc.date.available 2010-01-06T21:19:06Z
dc.date.issued 2005 en_US
dc.date.submitted 2005 Fall en
dc.identifier.other RegniC-121605-D3111 en_US
dc.identifier.uri http://hdl.handle.net/10355/4134
dc.description The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. en_US
dc.description Title from title screen of research.pdf file (viewed on October 18, 2007) en_US
dc.description Vita. en_US
dc.description Includes bibliographical references. en_US
dc.description Thesis (Ph. D.) University of Missouri-Columbia 2005. en_US
dc.description Dissertations, Academic -- University of Missouri--Columbia -- Biochemisty (Agriculture) en_US
dc.description.abstract The human pathogen Pseudomonas aeruginosa expresses a variety of cell surface polysaccharides, including alginate, lipopolysaccharide (LPS), and rhamnolipid. P. aeruginosa is the primary cause of chronic lung infections in cystic fibrosis (CF) patients, and these molecules contribute to its virulence. This dual-specificity enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) is required for the production of these molecules. The structure of PMM/PGM was previously solved in our laboratory, showing that the protein has four domains organized in a "heart shape," with the active site in a deep cleft formed by residues from each domain. Recently, we have determined the structures of PMM/PGM bound to its two substrates, two products, and an intermediate at 2.0 Å resolution or higher. These structures reveal the structural basis for diverse substrate recognition by the enzyme and pinpoint residues important for accomplishing the dynamic reorientation step of the reaction. en_US
dc.language.iso en_US en_US
dc.publisher University of Missouri--Columbia en_US
dc.subject phosphomannomutase/phosphoglucomutase. en_US
dc.subject phosphomannomutase/phosphoglucomutase en_US
dc.subject.lcsh Pseudomonas aeruginosa infections en_US
dc.subject.lcsh Cystic fibrosis -- Patients en_US
dc.title Structural studies of PMM/PGM from Pseudomonas aeruginosa en_US
dc.type Thesis en_US
thesis.degree.discipline Biochemistry (Agriculture) en_US
thesis.degree.grantor University of Missouri--Columbia en_US
thesis.degree.name Ph. D. en_US
thesis.degree.level Doctoral en_US
dc.identifier.merlin .b60595930 en_US
dc.identifier.oclc 174972669 en_US
dc.relation.ispartofcommunity University of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2005 Dissertations
dc.relation.ispartofcollection 2005 Freely available dissertations (MU)


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