PDBsum entry 1liq

Protein binding

PDB id: 1liq

Contents

Protein chain

27 a.a.

Metals

_ZN

PDB id:

1liq

Name:

Protein binding

Title:

Non-native solution structure of a fragment of the ch1 domain of cbp

Structure:

Creb binding protein. Chain: a. Fragment: residues 1-27. Engineered: yes

Source:

Synthetic: yes. Other_details: this sequence occurs naturally in humans

NMR struc:

20 models

Authors:

B.K.Sharpe,J.M.Matthews,A.H.Y.Kwan,A.Newton,D.A.Gell,M.Crossley, J.P.Mackay

Key ref:

B.K.Sharpe et al. (2002). A new zinc binding fold underlines the versatility of zinc binding modules in protein evolution. Structure, 10, 639-648. PubMed id: 12015147 DOI: 10.1016/S0969-2126(02)00757-8

Date:

18-Apr-02 Release date: 29-May-02

Protein chain

Q92793  (CBP_HUMAN) -  CREB-binding protein from Homo sapiens

Seq: 2442 a.a.

Struc: 27 a.a.

Enzyme reactions

• Enzyme class 1: E.C.2.3.1.- - ?????
• Enzyme class 2: 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: 10.1016/S0969-2126(02)00757-8

Structure 10:639-648 (2002)

PubMed id: 12015147

A new zinc binding fold underlines the versatility of zinc binding modules in protein evolution.

B.K.Sharpe, J.M.Matthews, A.H.Kwan, A.Newton, D.A.Gell, M.Crossley, J.P.Mackay.

ABSTRACT

Many different zinc binding modules have been identified. Their abundance and variety suggests that the formation of zinc binding folds might be relatively common. We have determined the structure of CH1(1), a 27-residue peptide derived from the first cysteine/histidine-rich region (CH1) of CREB binding protein (CBP). This peptide forms a highly ordered zinc-dependent fold that is distinct from known folds. The structure differs from a subsequently determined structure of a larger region from the CH3 region of CBP, and the CH1(1) fold probably represents a nonphysiologically active form. Despite this, the fold is thermostable and tolerant to both multiple alanine mutations and changes in the zinc-ligand spacing. Our data support the idea that zinc binding domains may arise frequently. Additionally, such structures may prove useful as scaffolds for protein design, given their stability and robustness.

Selected figure(s)

Figure 3.
Figure 3. Solution Structure of CH1[1](A) Stereoviews of the best 20 structures. Structures are superimposed for best fit over backbone atoms of residues 1-23 (note that residues 25-27 are not displayed, for clarity). Zinc-ligating side chains, red; zinc atom, gray; side chains of well-defined residues (2, 4, 7, 9, 12, 16, 21, and 22), green.(B) Ribbon diagram of the lowest energy structure of CH1[1]. The secondary structural elements recognized by the program MOLMOL [33] are shown.(C) Schematic zinc binding domain. Zinc binding domains can generally be thought of as two bidentate zinc-ligating motifs separated by an intervening sequence of highly variable length.(D) Overlay of the C-X[4]-C motifs in CH1[1] and TAZ2. Residues 5-10 of CH1[1] have been overlayed with residues 28-33 of TAZ2 (yellow) using the backbone atoms only. The rmsd is 0.42 Å.(E) Overlay of the H-X[3]-C motifs in CH1[1] and TAZ2. Residues 16-23 of CH1[1] have been overlayed with residues 39-46 of TAZ2 (yellow) using the backbone atoms only. The rmsd is 0.43 Å.

The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 639-648) copyright 2002.

Figure was selected by the author.