PDBsum entry: 2cu7

Transcription

PDB id: 2cu7

Contents

Protein chain

72 a.a. *

* Residue conservation analysis

PDB id:

2cu7

Name:

Transcription

Title:

Solution structure of the sant domain of human kiaa1915 protein

Structure:

Kiaa1915 protein. Chain: a. Fragment: sant domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kiaa1915. Other_details: cell-free protein synthesis

NMR struc:

20 models

Authors:

M.Yoneyama,T.Umehara,K.Saito,N.Tochio,S.Koshiba,M.Inoue, A.Tanaka,T.Kigawa,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

M.Yoneyama et al. (2007). Structural and Functional Differences of SWIRM Domain Subtypes. J Mol Biol, 369, 222-238. PubMed id: 17428495 DOI: 10.1016/j.jmb.2007.03.027

Date:

25-May-05 Release date: 25-Nov-05

Protein chain

Q5VVJ2  (MYSM1_HUMAN) -  Histone H2A deubiquitinase MYSM1

Seq: 828 a.a.

Struc: 72 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biological process: regulation of transcription (1 term)
• Biochemical function: DNA binding (1 term)

DOI no: 10.1016/j.jmb.2007.03.027

J Mol Biol 369:222-238 (2007)

PubMed id: 17428495

Structural and Functional Differences of SWIRM Domain Subtypes.

M.Yoneyama, N.Tochio, T.Umehara, S.Koshiba, M.Inoue, T.Yabuki, M.Aoki, E.Seki, T.Matsuda, S.Watanabe, Y.Tomo, Y.Nishimura, T.Harada, T.Terada, M.Shirouzu, Y.Hayashizaki, O.Ohara, A.Tanaka, T.Kigawa, S.Yokoyama.

ABSTRACT

SWIRM is a conserved domain found in several chromatin-associated proteins. Based on their sequences, the SWIRM family members can be classified into three subfamilies, which are represented by Swi3, LSD1, and Ada2. Here we report the SWIRM structure of human MYb-like, Swirm and Mpn domain-containing protein-1 (MYSM1). The MYSM1 SWIRM structure forms a compact HTH-related fold comprising five alpha-helices, which best resembles the Swi3 SWIRM structure, among the known SWIRM structures. The MYSM1 and Swi3 SWIRM structures are more similar to the LSD1 structure than the Ada2alpha structure. The SWIRM domains of MYSM1 and LSD1 lacked DNA binding activity, while those of Ada2alpha and the human Swi3 counterpart, SMARCC2, bound DNA. The dissimilarity in the DNA-binding ability of the MYSM1 and SMARCC2 SWIRM domains might be due to a couple of amino acid differences in the last helix. These results indicate that the SWIRM family has indeed diverged into three structural subfamilies (Swi3/MYSM1, LSD1, and Ada2 types), and that the Swi3/MYSM1-type subfamily has further diverged into two functionally distinct groups. We also solved the structure of the SANT domain of MYSM1, and demonstrated that it bound DNA with a similar mode to that of the c-Myb DNA-binding domain.

Selected figure(s)

Figure 1.
Figure 1. Schematic representations of the SWIRM domains. The MYSM1/SMARCC2, Ada2, and LSD1-types of the SWIRM family are shown with the representative SWIRM-containing proteins. Blue, yellow, red, light blue, and green indicate the putative zinc finger, SANT, SWIRM, JAMM, and histone demethylase domains, respectively. The amino acid length of each protein is shown on the right.

Figure 2.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 369, 222-238) copyright 2007.

Figures were selected by an automated process.