PDBsum entry 2lua

DNA binding protein

PDB id: 2lua

Contents

Protein chain

52 a.a.

Metals

_ZN ×3

PDB id:

2lua

Name:

DNA binding protein

Title:

Solution structure of cxc domain of msl2

Structure:

Protein male-specific lethal-2. Chain: a. Fragment: cxc domain. Engineered: yes. Mutation: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: msl-2, cg3241. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

Y.Feng,K.Ye,S.Zheng,J.Wang

Key ref:

S.Zheng et al. (2012). Solution structure of MSL2 CXC domain reveals an unusual Zn3Cys9 cluster and similarity to pre-SET domains of histone lysine methyltransferases. Plos One, 7, e45437. PubMed id: 23029009

Date:

09-Jun-12 Release date: 17-Oct-12

Protein chain

P50534  (MSL2_DROME) -  E3 ubiquitin-protein ligase msl-2 from Drosophila melanogaster

Seq: 773 a.a.

Struc: 52 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.2.3.2.27 - RING-type E3 ubiquitin transferase.
• Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine

Plos One 7:e45437 (2012)

PubMed id: 23029009

Solution structure of MSL2 CXC domain reveals an unusual Zn3Cys9 cluster and similarity to pre-SET domains of histone lysine methyltransferases.

S.Zheng, J.Wang, Y.Feng, J.Wang, K.Ye.

ABSTRACT

The dosage compensation complex (DCC) binds to single X chromosomes in Drosophila males and increases the transcription level of X-linked genes by approximately twofold. Male-specific lethal 2 (MSL2) together with MSL1 mediates the initial recruitment of the DCC to high-affinity sites in the X chromosome. MSL2 contains a DNA-binding cysteine-rich CXC domain that is important for X targeting. In this study, we determined the solution structure of MSL2 CXC domain by NMR spectroscopy. We identified three zinc ions in the CXC domain and determined the metal-to-cysteine connectivities from (1)H-(113)Cd correlation experiments. The structure reveals an unusual zinc-cysteine cluster composed of three zinc ions coordinated by six terminal and three bridging cysteines. The CXC domain exhibits unexpected structural homology to pre-SET motifs of histone lysine methyltransferases, expanding the distribution and structural diversity of the CXC domain superfamily. Our findings provide novel structural insight into the evolution and function of CXC domains.