1aoy

From Proteopedia

(Difference between revisions)

Revision as of 19:54, 24 December 2014

N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23 STRUCTURES

Structural highlights

1aoy is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ARGR_ECOLI] Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of the monomeric DNA-binding domain of the Escherichia coli arginine repressor, ArgR, determined by NMR spectroscopy, shows structural homology to the winged helix-turn-helix (wHTH) family, a motif found in a diverse class of proteins including both gene regulators and gene organizers from prokaryotes and eukaryotes. Biochemical data on DNA binding by intact ArgR are used as constraints to position the domain on its DNA target and to derive a model for the hexamer-DNA complex using the known structure of the L-arginine-binding domain. The structural independence of the wHTH fold may be important for multimeric DNA-binding proteins that contact extended DNA regions with imperfect match to consensus sequences, a feature of many wHTH-domain proteins.

Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA.,Sunnerhagen M, Nilges M, Otting G, Carey J Nat Struct Biol. 1997 Oct;4(10):819-26. PMID:9334747^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sunnerhagen M, Nilges M, Otting G, Carey J. Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA. Nat Struct Biol. 1997 Oct;4(10):819-26. PMID:9334747

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aoy"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aoy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aoy RCSB], [http://www.ebi.ac.uk/pdbsum/1aoy PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ARGR_ECOLI ARGR_ECOLI]] Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1aoy

From Proteopedia

Revision as of 19:54, 24 December 2014

N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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