PDBsum entry 1ztp

Structural genomics, unknown function

PDB id: 1ztp

Contents

Protein chain

228 a.a. *

Waters ×217

* Residue conservation analysis

PDB id:

1ztp

Name:

Structural genomics, unknown function

Title:

X-ray structure of gene product from homo sapiens hs.433573

Structure:

Basophilic leukemia expressed protein bles03. Chain: a, b, c. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: hs.433573. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.50Å R-factor: 0.191 R-free: 0.245

Authors:

G.E.Wesenberg,G.N.Phillips Jr.,E.Bitto,C.A.Bingman,S.T.M.Allard, Center For Eukaryotic Structural Genomics (Cesg)

Key ref:

E.Bitto et al. (2005). The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03. Acta Crystallograph Sect F Struct Biol Cryst Commun, 61, 812-817. PubMed id: 16511166 DOI: 10.1107/S1744309105023845

Date:

27-May-05 Release date: 14-Jun-05

Protein chains

Q9H3H3  (CK068_HUMAN) -  UPF0696 protein C11orf68 from Homo sapiens

Seq: 292 a.a.

Struc: 228 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1107/S1744309105023845

Acta Crystallograph Sect F Struct Biol Cryst Commun 61:812-817 (2005)

PubMed id: 16511166

The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03.

E.Bitto, C.A.Bingman, H.Robinson, S.T.Allard, G.E.Wesenberg, G.N.Phillips.

ABSTRACT

The crystal structure of the human basophilic leukemia-expressed protein (BLES03, p5326, Hs.433573) was determined by single-wavelength anomalous diffraction and refined to an R factor of 18.8% (Rfree = 24.5%) at 2.5 A resolution. BLES03 shows no detectable sequence similarity to any functionally characterized proteins using state-of-the-art sequence-comparison tools. The structure of BLES03 adopts a fold similar to that of eukaryotic transcription initiation factor 4E (eIF4E), a protein involved in the recognition of the cap structure of eukaryotic mRNA. In addition to fold similarity, the electrostatic surface potentials of BLES03 and eIF4E show a clear conservation of basic and acidic patches. In the crystal lattice, the acidic amino-terminal helices of BLES03 monomers are bound within the basic cavity of symmetry-related monomers in a manner analogous to the binding of mRNA by eIF4E. Interestingly, the gene locus encoding BLES03 is located between genes encoding the proteins DRAP1 and FOSL1, both of which are involved in transcription initiation. It is hypothesized that BLES03 itself may be involved in a biochemical process that requires recognition of nucleic acids.

Selected figure(s)

Figure 1.
Figure 1 (a) A topology diagram of the BLES03 structure (PDB code 1ztp ). The central nine-stranded -sheet (red) is surrounded by several helices (cyan). The figure was prepared using TopDraw based on a topology analysis of the BLES03 structure by the TOPS server (Bond, 2003[Bond, C. S. (2003). Bioinformatics, 19, 311-312.]; Westhead et al., 1999[Westhead, D. R., Slidel, T. W., Flores, T. P. & Thornton, J. M. (1999). Protein Sci. 8, 897-904.]). (b) A ribbon diagram of the BLES03 structure. The structure is labeled and colored to match the topology diagram. The figure was generated using PyMol (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org .]).

Figure 2.
Figure 2 Structural superposition of monomer B of human BLES03 (cyan; PDB code 1ztp ) and mouse eIF4E (red; PDB code 1eh1 ). The orientation of the structures is consistent with that introduced in Fig. 1-. The figure was generated using PyMol based on the structural alignment of proteins by DALI (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org .]; Holm & Sander, 1993[Holm, L. & Sander, C. (1993). J. Mol. Biol. 233, 123-138.]).

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2005, 61, 812-817) copyright 2005.

Figures were selected by an automated process.