 |
PDBsum entry 5ix1
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
5ix1
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Mouse morc3 is a ghkl atpase that localizes to h3k4me3 marked chromatin.
|
|
|
Authors
|
|
S.Li,
L.Yen,
W.A.Pastor,
J.B.Johnston,
J.Du,
C.J.Shew,
W.Liu,
J.Ho,
B.Stender,
A.T.Clark,
A.L.Burlingame,
L.Daxinger,
D.J.Patel,
S.E.Jacobsen.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 2016,
113,
E5108.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Microrchidia (MORC) proteins are GHKL (gyrase, heat-shock protein 90, histidine
kinase, MutL) ATPases that function in gene regulation in multiple organisms.
Animal MORCs also contain CW-type zinc finger domains, which are known to bind
to modified histones. We solved the crystal structure of the murine MORC3
ATPase-CW domain bound to the nucleotide analog AMPPNP (phosphoaminophosphonic
acid-adenylate ester) and in complex with a trimethylated histone H3 lysine 4
(H3K4) peptide (H3K4me3). We observed that the MORC3 N-terminal ATPase domain
forms a dimer when bound to AMPPNP. We used native mass spectrometry to show
that dimerization is ATP-dependent, and that dimer formation is enhanced in the
presence of nonhydrolyzable ATP analogs. The CW domain uses an aromatic cage to
bind trimethylated Lys4 and forms extensive hydrogen bonds with the H3 tail. We
found that MORC3 localizes to promoters marked by H3K4me3 throughout the genome,
consistent with its binding to H3K4me3 in vitro. Our work sheds light on aspects
of the molecular dynamics and function of MORC3.
|
|
|
|
|
|
|
