PDBsum entry 4xoi

Cell cycle

PDB id: 4xoi

Contents

Protein chains

177 a.a.

210 a.a.

Ligands

GTP ×2

Metals

_MG ×2

Waters ×417

PDB id:

4xoi

Name:

Cell cycle

Title:

Structure of hsanillin bound with rhoa(q63l) at 2.1 angstroms resolution

Structure:

Transforming protein rhoa. Chain: a, c. Fragment: unp residues 1-180. Synonym: rho cdna clone 12,h12. Engineered: yes. Mutation: yes. Actin-binding protein anillin. Chain: b, d. Fragment: rbd domain, unp residues 712-981.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rhoa, arh12, arha, rho12. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: anln.

Resolution:

2.09Å R-factor: 0.174 R-free: 0.206

Authors:

L.Sun,R.Guan,I.-J.Lee,Y.Liu,M.Chen,J.Wang,J.Wu,Z.Chen

Key ref:

L.Sun et al. (2015). Mechanistic insights into the anchorage of the contractile ring by anillin and Mid1. Dev Cell, 33, 413-426. PubMed id: 25959226 DOI: 10.1016/j.devcel.2015.03.003

Date:

16-Jan-15 Release date: 15-Jul-15

Protein chains

P61586  (RHOA_HUMAN) -  Transforming protein RhoA from Homo sapiens

Seq: 193 a.a.

Struc: 177 a.a.*

Protein chains

Q9NQW6  (ANLN_HUMAN) -  Anillin from Homo sapiens

Seq: 1124 a.a.

Struc: 210 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chains A, C: E.C.3.6.5.2 - small monomeric GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

GTP (Bound ligand (Het Group name = GTP) corresponds exactly) + H2O = GDP + phosphate + H(+)

• Enzyme class 3: Chains B, D: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.devcel.2015.03.003

Dev Cell 33:413-426 (2015)

PubMed id: 25959226

Mechanistic insights into the anchorage of the contractile ring by anillin and Mid1.

L.Sun, R.Guan, I.J.Lee, Y.Liu, M.Chen, J.Wang, J.Q.Wu, Z.Chen.

ABSTRACT

Anillins and Mid1 are scaffold proteins that play key roles in anchorage of the contractile ring at the cell equator during cytokinesis in animals and fungi, respectively. Here, we report crystal structures and functional analysis of human anillin and S. pombe Mid1. The combined data show anillin contains a cryptic C2 domain and a Rho-binding domain. Together with the tethering PH domain, three membrane-associating elements synergistically bind to RhoA and phospholipids to anchor anillin at the cleavage furrow. Surprisingly, Mid1 also binds to the membrane through a cryptic C2 domain. Dimerization of Mid1 leads to high affinity and preference for PI(4,5)P2, which stably anchors Mid1 at the division plane, bypassing the requirement for Rho GTPase. These findings uncover the unexpected general machinery and the divergent regulatory logics for the anchorage of the contractile ring through the anillin/Mid1 family proteins from yeast to humans.