PDBsum entry: 1zir

Structural protein

PDB id: 1zir

Contents

Protein chain

173 a.a. *

Ligands

ACT ×3

Waters ×147

* Residue conservation analysis

PDB id:

1zir

Name:

Structural protein

Title:

Deuterated gammae crystallin in h2o solvent

Structure:

Gamma crystallin e. Chain: a. Synonym: gamma crystallin 3-1, gamma-2. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.36Å R-factor: 0.187 R-free: 0.211

Authors:

J.B.Artero,M.Hartlein,S.Mcsweeney,P.Timmins

Key ref:

J.B.Artero et al. (2005). A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O. Acta Crystallogr D Biol Crystallogr, 61, 1541-1549. PubMed id: 16239733 DOI: 10.1107/S0907444905028532

Date:

27-Apr-05 Release date: 08-Nov-05

Protein chain

P02528  (CRGE_RAT) -  Gamma-crystallin E

Seq: 174 a.a.

Struc: 173 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: lens development in camera-type eye (1 term)
• Biochemical function: structural constituent of eye lens (1 term)

DOI no: 10.1107/S0907444905028532

Acta Crystallogr D Biol Crystallogr 61:1541-1549 (2005)

PubMed id: 16239733

A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O.

J.B.Artero, M.Härtlein, S.McSweeney, P.Timmins.

ABSTRACT

Rat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values.

Selected figure(s)

Figure 1.
Figure 1 2F[o] - F[c] electron-density map of the cd loop of Greek-key motif 3 of D [gamma] E-H[2]O. (a) Representation of the double conformation of residues Phe115 and His166 with the electron density at 1 [sigma] . (b) The aromatic rings of the Phe117 residues are located in the same position but the C^ [alpha] and C^ [beta] atoms are displaced. All C atoms of the loop are shown in ball-and-stick representation in light yellow for the first conformation and in purple in the second conformation. N atoms are in blue and O atoms are in red. The figures were prepared using PyMOL (DeLano, 2002 [DeLano, W. (2002). The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA.]-[bluearr.gif] ).

Figure 5.
Figure 5 Ball-and stick representation of the hydrophobic core maintained by phenylalanines 116, 118, 121 and 125 in the two conformations of the cd loop. Despite the double conformation, aromatic residues present their side chains at approximately the same position. All C atoms of the loop are shown in light yellow for the first conformation and in purple for the second conformation. N atoms are in blue and O atoms in red. The figures were prepared using PyMOL (DeLano, 2002 [DeLano, W. (2002). The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA.]-[bluearr.gif] ).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2005, 61, 1541-1549) copyright 2005.

Figures were selected by the author.