PDBsum entry 2frs

Transport protein

PDB id: 2frs

Contents

Protein chains

124 a.a. *

133 a.a. *

Metals

_NA ×4

Waters ×468

* Residue conservation analysis

PDB id:

2frs

Name:

Transport protein

Title:

Crystal structure of the f15w mutant of apo-cellular retinoic acid binding protein type ii at 1.51 angstroms resolution

Structure:

Cellular retinoic acid-binding protein 2. Chain: a, b. Synonym: cellular retinoic acid- binding protein ii, crabp-ii, retinoic acid-binding protein ii, cellular. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: crabp2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.51Å R-factor: 0.180 R-free: 0.240

Authors:

S.Vaezeslami,J.H.Geiger

Key ref:

S.Vaezeslami et al. (2006). The structure of Apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation. J Mol Biol, 363, 687-701. PubMed id: 16979656 DOI: 10.1016/j.jmb.2006.08.059

Date:

20-Jan-06 Release date: 19-Sep-06

Protein chain

P29373  (RABP2_HUMAN) -  Cellular retinoic acid-binding protein 2 from Homo sapiens

Seq: 138 a.a.

Struc: 124 a.a.*

Protein chain

P29373  (RABP2_HUMAN) -  Cellular retinoic acid-binding protein 2 from Homo sapiens

Seq: 138 a.a.

Struc: 133 a.a.*

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

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1016/j.jmb.2006.08.059

J Mol Biol 363:687-701 (2006)

PubMed id: 16979656

The structure of Apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation.

S.Vaezeslami, E.Mathes, C.Vasileiou, B.Borhan, J.H.Geiger.

ABSTRACT

CRABPII is a small, cytosolic protein that solubilizes and transfers retinoic acid (RA) to the nucleus while also enhancing its transcriptional activity. We have determined the first high-resolution structure of apo-wild type (WT) CRABPII at 1.35 A. Using three different data sets collected on apo-WT CRABPII we have shown that apo- and holo-CRABPII share very similar structures. Binding of RA appears to increase the overall rigidity of the structure, although the induced structural changes are not as pronounced as previously thought. The enhanced structural rigidity may be an important determinant for the enhanced nuclear localization of the RA-bound protein. Comparison of our apo-WT with a mutant apo-CRABPII structure shows that mutation of Arg111, a conserved residue of CRABPII and a key residue in RA binding, causes structural changes in the molecule. We further investigated the structural importance of conserved residues by determining the structure of the F15W mutant CRABPII (F15W-CRABPII). Our structures also demonstrate structural changes induced by crystal packing and show that a crystal can harbor demonstrative structural differences in the asymmetric unit.

Selected figure(s)

Figure 2.
Figure 2. Structural differences between the two molecules in the asymmetric unit of apo-CRABPII. Superimposed structures of Mol A (green) and Mol B (hot pink) of Xtal1. Figure 2. Structural differences between the two molecules in the asymmetric unit of apo-CRABPII. Superimposed structures of Mol A (green) and Mol B (hot pink) of Xtal1.

Figure 4.
Figure 4. The significant structural consequences of the R111M mutation. (a) Mol A's of R111M (red) and Xtal1 (green); and (b) Mol B's of R111M (blue) and Xtal1 (hot pink) are superimposed. Figure 4. The significant structural consequences of the R111M mutation. (a) Mol A's of R111M (red) and Xtal1 (green); and (b) Mol B's of R111M (blue) and Xtal1 (hot pink) are superimposed.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2006, 363, 687-701) copyright 2006.

Figures were selected by an automated process.