1h9s
From Proteopedia
(New page: 200px<br /> <applet load="1h9s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h9s, resolution 1.82Å" /> '''MOLYBDATE BOUND COM...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H9S is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from | + | 1H9S is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with MOO as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H9S OCA]]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: transcription regulator]] | [[Category: transcription regulator]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:20:19 2007'' |
Revision as of 12:15, 30 October 2007
|
MOLYBDATE BOUND COMPLEX OF DIMOP DOMAIN OF MODE FROM E.COLI
Overview
The molybdate-dependent transcriptional regulator ModE of Escherichia coli, functions as a sensor of intracellular molybdate concentration and a, regulator for the transcription of several operons that control the uptake, and utilization of molybdenum. We present two high-resolution crystal, structures of the C-terminal oxyanion-binding domain in complex with, molybdate and tungstate. The ligands bind between subunits at the, dimerization interface, and analysis reveals that oxyanion selectivity is, determined primarily by size. The relevance of the structures is indicated, by fluorescence measurements, which show that the oxyanion binding, properties of the C-terminal domain of ModE are similar to those of the, full-length protein. Comparisons with the apoprotein structure have, ... [(full description)]
About this Structure
1H9S is a [Protein complex] structure of sequences from [Escherichia coli] with MOO as [ligand]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [OCA].
Reference
Oxyanion binding alters conformation and quaternary structure of the c-terminal domain of the transcriptional regulator mode. Implications for molybdate-dependent regulation, signaling, storage, and transport., Gourley DG, Schuttelkopf AW, Anderson LA, Price NC, Boxer DH, Hunter WN, J Biol Chem. 2001 Jun 8;276(23):20641-7. Epub 2001 Mar 20. PMID:11259434
Page seeded by OCA on Tue Oct 30 14:20:19 2007
