PDBsum entry 5hj0

Ligase

PDB id: 5hj0

Contents

Protein chains

100 a.a.

Metals

_ZN ×3

Waters ×10

PDB id:

5hj0

Name:

Ligase

Title:

Crystal structure of mis18 'yippee-like' domain

Structure:

Kinetochore protein mis18. Chain: a, b, c. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Gene: mis18, spcc970.12. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.64Å R-factor: 0.222 R-free: 0.260

Authors:

B.Medina-Pritchard,L.Subramanian,R.Allshire,A.Arockia Jeyaprakash

Key ref:

L.Subramanian et al. (2016). Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization. Embo Rep, 17, 496-507. PubMed id: 26921242 DOI: 10.15252/embr.201541520

Date:

12-Jan-16 Release date: 09-Mar-16

Protein chains

Q9P802  (MIS18_SCHPO) -  Kinetochore protein mis18 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 194 a.a.

Struc: 100 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.15252/embr.201541520

Embo Rep 17:496-507 (2016)

PubMed id: 26921242

Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization.

L.Subramanian, B.Medina-Pritchard, R.Barton, F.Spiller, R.Kulasegaran-Shylini, G.Radaviciute, R.C.Allshire, A.Arockia Jeyaprakash.

ABSTRACT

Mis18 is a key regulator responsible for the centromere localization of the CENP-A chaperone Scm3 in Schizosaccharomyces pombe and HJURP in humans, which establishes CENP-A chromatin that defines centromeres. The molecular and structural determinants of Mis18 centromere targeting remain elusive. Here, by combining structural, biochemical, and yeast genetic studies, we show that the oligomerization of S. pombe Mis18, mediated via its conserved N-terminal Yippee-like domain, is crucial for its centromere localization and function. The crystal structure of the N-terminal Yippee-like domain reveals a fold containing a cradle-shaped pocket that is implicated in protein/nucleic acid binding, which we show is required for Mis18 function. While the N-terminal Yippee-like domain forms a homodimer in vitro and in vivo, full-length Mis18, including the C-terminal α-helical domain, forms a homotetramer in vitro We also show that the Yippee-like domains of human Mis18α/Mis18β interact to form a heterodimer, implying a conserved structural theme for Mis18 regulation.