2cfx: Difference between revisions
New page: left|200px<br /><applet load="2cfx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cfx, resolution 2.40Å" /> '''STRUCTURE OF B.SUBTI... |
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[[Image:2cfx.gif|left|200px]]<br /><applet load="2cfx" size=" | [[Image:2cfx.gif|left|200px]]<br /><applet load="2cfx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2cfx, resolution 2.40Å" /> | caption="2cfx, resolution 2.40Å" /> | ||
'''STRUCTURE OF B.SUBTILIS LRPC'''<br /> | '''STRUCTURE OF B.SUBTILIS LRPC'''<br /> | ||
==Overview== | ==Overview== | ||
The Lrp/AsnC family of transcriptional regulatory proteins is found in | The Lrp/AsnC family of transcriptional regulatory proteins is found in both archaea and bacteria. Members of the family influence cellular metabolism in both a global (Lrp) and specific (AsnC) manner, often in response to exogenous amino acid effectors. In the present study we have determined both the first bacterial and the highest resolution structures for members of the family. Escherichia coli AsnC is a specific gene regulator whose activity is triggered by asparagine binding. Bacillus subtilis LrpC is a global regulator involved in chromosome condensation. Our AsnC-asparagine structure is the first for a regulator-effector complex and is revealed as an octameric disc. Key ligand recognition residues are identified together with a route for ligand access. The LrpC structure reveals a stable octamer supportive of a topological role in dynamic DNA packaging. The structures yield significant clues to the functionality of Lrp/AsnC-type regulators with respect to ligand binding and oligomerization states as well as to their role in specific and global DNA regulation. | ||
==About this Structure== | ==About this Structure== | ||
2CFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | 2CFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Rafferty, J | [[Category: Rafferty, J B.]] | ||
[[Category: Thaw, P.]] | [[Category: Thaw, P.]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
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[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:12 2008'' | ||
Revision as of 17:48, 21 February 2008
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STRUCTURE OF B.SUBTILIS LRPC
OverviewOverview
The Lrp/AsnC family of transcriptional regulatory proteins is found in both archaea and bacteria. Members of the family influence cellular metabolism in both a global (Lrp) and specific (AsnC) manner, often in response to exogenous amino acid effectors. In the present study we have determined both the first bacterial and the highest resolution structures for members of the family. Escherichia coli AsnC is a specific gene regulator whose activity is triggered by asparagine binding. Bacillus subtilis LrpC is a global regulator involved in chromosome condensation. Our AsnC-asparagine structure is the first for a regulator-effector complex and is revealed as an octameric disc. Key ligand recognition residues are identified together with a route for ligand access. The LrpC structure reveals a stable octamer supportive of a topological role in dynamic DNA packaging. The structures yield significant clues to the functionality of Lrp/AsnC-type regulators with respect to ligand binding and oligomerization states as well as to their role in specific and global DNA regulation.
About this StructureAbout this Structure
2CFX is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
ReferenceReference
Structural insight into gene transcriptional regulation and effector binding by the Lrp/AsnC family., Thaw P, Sedelnikova SE, Muranova T, Wiese S, Ayora S, Alonso JC, Brinkman AB, Akerboom J, van der Oost J, Rafferty JB, Nucleic Acids Res. 2006 Mar 9;34(5):1439-49. Print 2006. PMID:16528101
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