PDBsum entry 3zil

Cell cycle

PDB id

3zil

Loading ...

Contents

			Protein chains

					362 a.a.


					11 a.a.

			Waters ×61

PDB id:

3zil

Links

Name:

Cell cycle

Title:

Structure of the wpl1 protein

Structure:

Aar187cp. Chain: a. Fragment: residues 184-561. Synonym: wpl1. Engineered: yes. Aal182wp. Chain: b. Fragment: residues 136-163. Synonym: smc3.

Source:

Eremothecium gossypii. Organism_taxid: 33169. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 33169

Resolution:

2.01Å

R-factor:

0.202

R-free:

0.246

Authors:

A.Chatterjee,S.Zakian,X.-W.Hu,M.R.Singleton

Key ref:

A.Chatterjee et al. (2013). Structural insights into the regulation of cohesion establishment by Wpl1. Embo J, 32, 677-687. PubMed id: 23395900 DOI: 10.1038/emboj.2013.16

Date:

09-Jan-13

Release date:

20-Feb-13

PROCHECK

	Headers

	References

Protein chain

Q75E93 (Q75E93_ASHGO) - AAR187Cp from Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)

Seq: Struc:

Seq: Struc:					561 a.a. 362 a.a.

Protein chain

Q75FB3 (Q75FB3_ASHGO) - Structural maintenance of chromosomes protein from Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)

Seq: Struc:

Seq: Struc:

Seq: Struc:					1231 a.a. 11 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1038/emboj.2013.16	Embo J 32:677-687 (2013)
PubMed id: 23395900

Structural insights into the regulation of cohesion establishment by Wpl1.
A.Chatterjee, S.Zakian, X.W.Hu, M.R.Singleton.

ABSTRACT

Correct segregation of duplicated chromosomes to daughter cells during mitosis requires the action of the cohesin complex. This tripartite ring-shaped molecule is involved in holding replicated sister chromatids together from S phase until anaphase onset. Establishment of stable cohesion involves acetylation of the Smc3 component of cohesin during replication by the Eco1 acetyltransferase. This has been proposed to antagonise the activity of another member of the cohesin complex, Wpl1. Here, we describe the X-ray structure of the conserved Wapl domain, and demonstrate that it binds the ATPase head of the Smc3 protein. We present data that suggest that Wpl1 may be involved in regulating the ATPase activity of cohesin, and that this may be subject to the acetylation state of Smc3. In addition, we present a structure of the Wapl domain bound to a functionally relevant segment of the Smc3 ATPase.