Structure determination of a mercury binding protein, MERP / Ruth Steele.

Format:

Book

Manuscript

Microformat

Thesis/Dissertation

Author/Creator:

Steele, Ruth.

Contributor:

University of Pennsylvania.

Language:

English

Subjects (All):

Penn dissertations--Chemistry.

Chemistry--Penn dissertations.

Local Subjects:

Penn dissertations--Chemistry.

Chemistry--Penn dissertations.

Physical Description:

x, 81 pages : illustrations ; 29 cm

Production:

1996.

Summary:

Bacteria with plasmids encoding the mercury detoxification system have the ability to transport Hg(II) across the cell membrane into the cell, where it is reduced to Hg(0) and passively eliminated. The net effect is to allow the bacteria to thrive in environments contaminated with toxic Hg(II) compounds. One protein involved in this process has been investigated by NMR spectroscopy. MerP (periplasmic) has 72 residues and binds Hg(II). The structure of two forms of merP (reduced and Hg$\sp{2+}$ bound) have been determined using triple resonance multidimensional solution NMR spectroscopy. Structural differences between the two forms of the protein are localized to the metal binding region containing the consensus sequence GMTCXXC. The protein has a $\beta\alpha\beta\beta\alpha\beta$ fold with the two $\alpha$ helices overlaying a four strand antiparallel $\beta$ sheet. Binding of a mercury ion to merP causes a hydrophobic Phe ring to move significantly. This may be involved in protein-protein recognition with another member of the mercury detoxification family, merT.

Notes:

Thesis (Ph.D. in Chemistry) -- University of Pennsylvania, 1996.

Includes bibliographical references.

Local Notes:

University Microfilms order no.: 97-13009.

OCLC:

187469460