PDBsum entry 1qli

Metal binding protein

PDB id: 1qli

Contents

Protein chain

59 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

1qli

Name:

Metal binding protein

Title:

Quail cysteine and glycine-rich protein, nmr, minimized average structure

Structure:

Cysteine and glycine-rich protein. Chain: a. Fragment: c-terminal lim domain residues 82 - 194. Synonym: qcrp2(lim2), zn(ii)-qcrp2(lim2). Engineered: yes

Source:

Coturnix japonica. Japanese quail. Organism_taxid: 93934. Cell_line: bl21. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

R.Konrat,R.Weiskirchen,B.Krautler,K.Bister

Key ref:

R.Konrat et al. (1997). Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2. J Biol Chem, 272, 12001-12007. PubMed id: 9115265 DOI: 10.1074/jbc.272.18.12001

Date:

17-Feb-97 Release date: 20-Aug-97

Protein chain

Q05158  (CSRP2_COTJA) -  Cysteine and glycine-rich protein 2 from Coturnix japonica

Seq: 194 a.a.

Struc: 59 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.272.18.12001

J Biol Chem 272:12001-12007 (1997)

PubMed id: 9115265

Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2.

R.Konrat, R.Weiskirchen, B.Kräutler, K.Bister.

ABSTRACT

Proteins of the cysteine-rich protein (CRP) family (CRP1, CRP2, and CRP3) are implicated in diverse processes linked to cellular differentiation and growth control. CRP proteins contain two LIM domains, each formed by two zinc-binding modules of the CCHC and CCCC type, respectively. The solution structure of the carboxyl-terminal LIM domain (LIM2) from recombinant quail CRP2 was determined by multidimensional homo- and heteronuclear magnetic resonance spectroscopy. The folding topology retains both independent zinc binding modules (CCHC and CCCC). Each module consists of two orthogonally arranged antiparallel beta-sheets, and the carboxyl-terminal CCCC module is terminated by an alpha-helix. 15N magnetic relaxation data indicate that the modules differ in terms of conformational flexibility. They pack together via a hydrophobic core region. In addition, Arg122 in the CCHC module and Glu155 in the CCCC module are linked by an intermodular hydrogen bond and/or salt bridge. These residues are absolutely conserved in the CRP family of LIM proteins, and their interaction might contribute to the relative orientation of the two zinc-binding modules in CRP LIM2 domains. The global fold of quail CRP2 LIM2 is very similar to that of the carboxyl-terminal LIM domain of the related but functionally distinct CRP family member CRP1, analyzed recently. The carboxyl-terminal CCCC module is structurally related to the DNA-binding domain of the erythroid transcription factor GATA-1. In the two zinc-binding modules of quail CRP2 LIM2, flexible loop regions made up of conserved amino acid residues are located on the same side of the LIM2 domain and may cooperate in macromolecular recognition.

Selected figure(s)

Figure 5.
Fig. 5. Solution structure of qCRP2(LIM2). Stereoview showing the overlay of 15 final structures of qCRP2(LIM2) for the central residues 118-174. All backbone heavy atoms (N, C[ ], and C ) are shown.

Figure 7.
Fig. 7. Superposition of qCRP2(LIM2) with corresponding residues of chicken CRP1(LIM2). A and B, comparison of the folding of the amino-terminal CCHC (A) and the carboxyl-terminal CCCC^ (B) module of qCRP2(LIM2) (shown in light blue) and chicken CRP1(LIM2) (shown in gray) (20).

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1997, 272, 12001-12007) copyright 1997.

Figures were selected by an automated process.