1odh: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 4: Line 4:


==Overview==
==Overview==
Glia cell missing (GCM) transcription factors form a small family of, transcriptional regulators in metazoans. The prototypical Drosophila GCM, protein directs the differentiation of neuron precursor cells into glia, cells, whereas mammalian GCM proteins are involved in placenta and, parathyroid development. GCM proteins share a highly conserved 150 amino, acid residue region responsible for DNA binding, known as the GCM domain., Here we present the crystal structure of the GCM domain from murine GCMa, bound to its octameric DNA target site at 2.85 A resolution. The GCM, domain exhibits a novel fold consisting of two domains tethered together, by one of two structural Zn ions. We observe the novel use of a beta-sheet, in DNA recognition, whereby a five- stranded beta-sheet protrudes into the, major groove perpendicular to the DNA axis. The structure combined with, mutational analysis of the target site and of DNA-contacting residues, provides insight into DNA recognition by this new type of Zn-containing, DNA-binding domain.
Glia cell missing (GCM) transcription factors form a small family of transcriptional regulators in metazoans. The prototypical Drosophila GCM protein directs the differentiation of neuron precursor cells into glia cells, whereas mammalian GCM proteins are involved in placenta and parathyroid development. GCM proteins share a highly conserved 150 amino acid residue region responsible for DNA binding, known as the GCM domain. Here we present the crystal structure of the GCM domain from murine GCMa bound to its octameric DNA target site at 2.85 A resolution. The GCM domain exhibits a novel fold consisting of two domains tethered together by one of two structural Zn ions. We observe the novel use of a beta-sheet in DNA recognition, whereby a five- stranded beta-sheet protrudes into the major groove perpendicular to the DNA axis. The structure combined with mutational analysis of the target site and of DNA-contacting residues provides insight into DNA recognition by this new type of Zn-containing DNA-binding domain.


==About this Structure==
==About this Structure==
Line 13: Line 13:
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Cohen, S.X.]]
[[Category: Cohen, S X.]]
[[Category: Muller, C.W.]]
[[Category: Muller, C W.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: dna-binding domain]]
[[Category: dna-binding domain]]
Line 20: Line 20:
[[Category: transcription factor]]
[[Category: transcription factor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:56:31 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:31 2008''

Revision as of 15:16, 21 February 2008

File:1odh.gif


1odh, resolution 2.85Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE GCM DOMAIN BOUND TO DNA

OverviewOverview

Glia cell missing (GCM) transcription factors form a small family of transcriptional regulators in metazoans. The prototypical Drosophila GCM protein directs the differentiation of neuron precursor cells into glia cells, whereas mammalian GCM proteins are involved in placenta and parathyroid development. GCM proteins share a highly conserved 150 amino acid residue region responsible for DNA binding, known as the GCM domain. Here we present the crystal structure of the GCM domain from murine GCMa bound to its octameric DNA target site at 2.85 A resolution. The GCM domain exhibits a novel fold consisting of two domains tethered together by one of two structural Zn ions. We observe the novel use of a beta-sheet in DNA recognition, whereby a five- stranded beta-sheet protrudes into the major groove perpendicular to the DNA axis. The structure combined with mutational analysis of the target site and of DNA-contacting residues provides insight into DNA recognition by this new type of Zn-containing DNA-binding domain.

About this StructureAbout this Structure

1ODH is a Protein complex structure of sequences from Mus musculus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition., Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Muller CW, EMBO J. 2003 Apr 15;22(8):1835-45. PMID:12682016

Page seeded by OCA on Thu Feb 21 14:16:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA