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1oi8
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(New page: 200px<br /> <applet load="1oi8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oi8, resolution 2.10Å" /> '''5'-NUCLEOTIDASE (E....)
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Revision as of 17:00, 29 October 2007
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5'-NUCLEOTIDASE (E. COLI) WITH AN ENGINEERED DISULFIDE BRIDGE (P90C, L424C)
Overview
Engineering disulfide bridges is a common technique to lock a protein, movement in a defined conformational state. We have designed two double, mutants of Escherichia coli 5'-nucleotidase to trap the enzyme in both an, open (S228C, P513C) and a closed (P90C, L424C) conformation by the, formation of disulfide bridges. The mutant proteins have been expressed, purified, and crystallized, to structurally characterize the designed, variants. The S228C, P513C is a double mutant crystallized in two, different crystal forms with three independent conformers, which differ, from each other by a rotation of up to 12 degrees of the C-terminal domain, with respect to the N-terminal domain. This finding, as well as an, analysis of the domain motion in the crystal, indicates that the enzyme, still ... [(full description)]
About this Structure
1OI8 is a [Single protein] structure of sequence from [Escherichia coli] with MN, SO4 and CO3 as [ligands]. Full crystallographic information is available from [OCA].
Reference
Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges., Schultz-Heienbrok R, Maier T, Strater N, Protein Sci. 2004 Jul;13(7):1811-22. PMID:15215524
Page seeded by OCA on Mon Oct 29 19:04:41 2007
