PDBsum entry 2c52

Transferase

PDB id: 2c52

Contents

Protein chains

58 a.a.

59 a.a. *

* Residue conservation analysis

PDB id:

2c52

Name:

Transferase

Title:

Structural diversity in cbp p160 complexes

Structure:

Creb-binding protein. Chain: a. Fragment: sid, residues 2059-2117. Engineered: yes. Nuclear receptor coactivator 1. Chain: b. Fragment: ad1, residues 920-970. Synonym: steroid receptor coactivator 1, ncoa-1, src-1, rip160, hin-2 protein.

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.

NMR struc:

37 models

Authors:

L.C.Waters,B.Yue,V.Veverka,P.S.Renshaw,J.Bramham,S.Matsuda, T.Frenkiel,G.Kelly,F.W.Muskett,M.D.Carr,D.M.Heery

Key ref:

L.Waters et al. (2006). Structural diversity in p160/CREB-binding protein coactivator complexes. J Biol Chem, 281, 14787-14795. PubMed id: 16540468 DOI: 10.1074/jbc.M600237200

Date:

25-Oct-05 Release date: 15-Mar-06

Protein chain

P45481  (CBP_MOUSE) -  Histone lysine acetyltransferase CREBBP from Mus musculus

Seq: 2441 a.a.

Struc: 58 a.a.*

Protein chain

Q15788  (NCOA1_HUMAN) -  Nuclear receptor coactivator 1 from Homo sapiens

Seq: 1441 a.a.

Struc: 59 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.2.3.1.- - ?????
• Enzyme class 2: Chains A, B: E.C.2.3.1.48 - histone acetyltransferase.
• Reaction: L-lysyl-[protein] + acetyl-CoA = N₆-acetyl-L-lysyl-[protein] + CoA + H⁺

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

Added reference

DOI no: 10.1074/jbc.M600237200

J Biol Chem 281:14787-14795 (2006)

PubMed id: 16540468

Structural diversity in p160/CREB-binding protein coactivator complexes.

L.Waters, B.Yue, V.Veverka, P.Renshaw, J.Bramham, S.Matsuda, T.Frenkiel, G.Kelly, F.Muskett, M.Carr, D.M.Heery.

ABSTRACT

Ligand-induced transcription by nuclear receptors involves the recruitment of p160 coactivators such as steroid receptor coactivator 1 (SRC1), in complex with histone acetyltransferases such as CREB-binding protein (CBP) and p300. Here we describe the solution structure of a complex formed by the SRC1 interaction domain (SID) of CBP and the activation domain (AD1) of SRC1, both of which contain four helical regions (Calpha1, Calpha2, Calpha3, and Calpha3' in CBP and Salpha1, Salpha2', Salpha2, and Salpha3 in SRC1). A tight four-helix bundle is formed between Salpha1, Calpha1, Calpha2, and Calpha3 that is capped by Salpha3. In contrast to the structure of the AD1 domain of the related p160 protein ACTR in complex with CBP SID, the sequences forming Salpha2' and Salpha2 in SRC1 AD1 are not involved in the interface between the two domains but rather serve to position Salpha3. Thus, although the CBP SID domain adopts a similar fold in complex with different p160 proteins, the topologies of the AD1 domains are strikingly different, a feature that is likely to contribute to functional specificity of these coactivator complexes.

Selected figure(s)

Figure 2.
FIGURE 2. Solution structure of the CBP SID-SRC1 AD1 complex. A, best fit superimposition of the family of 37 converged NMR structures obtained for the CBP SID-SRC1 AD1 complex. The CBP SID domain is shown in blue and SRC1 AD1 in red. B, schematic (ribbon) representation of the backbone topology of the two polypeptides in the complex, using the same orientation as in A, and demonstrating the tight 4-helix bundle conformation. The four helices of CBP SID (C 1, C 2, C 3, and C 3') and SRC1 AD1 (S 1, S 2',S 2, and S 3) are indicated, along with the N and C termini of both domains.

Figure 3.
FIGURE 3. Comparison of CBP SID/SRC1 AD1 and CBP SID-ACTR AD1 complexes. A and B, equivalent views of the backbone topology of the CBP SID-SRC1 AD1 and CBP SID-ACTR AD1 complexes, respectively, which were obtained by superimposing the CBP SID domain from both complexes (residues Ile^2063, Pro^2065-Ala^2067, Asp^2070-Ser^2079, and Gln^2085-Lys^2108). The CBP SID domain is shown in blue; SRC1 AD1 is shown in red and ACTR AD1 in green. C, comparison of the backbone topologies of the two CBP SID domains, which were overlaid on the same residues as in A and B. The CBP SID domains from the SRC1 AD1 and ACTR AD1 complexes are shown in blue and cyan, respectively. D, comparison of the backbone folds of the AD1 domains of SRC1 (red) and ACTR (yellow), which were overlaid on residues Ile^2063, Pro^2065-Ala^2067, Asp^2070-Ser^2079, Gln^2085-Lys^2108 of CBP-SID and residues Asp^928-Ser^941 and Asp^1044-Ser^1057 of SRC1 and ACTR, respectively.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 14787-14795) copyright 2006.

Figures were selected by the author.