PDBsum entry: 1pu1

Structural genomics, unknown function

PDB id: 1pu1

Contents

Protein chain

91 a.a.

PDB id:

1pu1

Name:

Structural genomics, unknown function

Title:

Solution structure of the hypothetical protein mth677 from methanothermobacter thermautotrophicus

Structure:

Hypothetical protein mth677. Chain: a. Engineered: yes

Source:

Methanothermobacter thermautotrophicus. Organism_taxid: 145262. Gene: mth677. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

30 models

Authors:

F.J.Blanco,A.Yee,R.Campos-Olivas,D.Devos,A.Valencia, C.H.Arrowsmith,M.Rico

Key ref:

F.J.Blanco et al. (2004). Solution structure of the hypothetical protein Mth677 from Methanobacterium thermoautotrophicum: a novel alpha+beta fold. Protein Sci, 13, 1458-1465. PubMed id: 15152082 DOI: 10.1110/ps.04620504

Date:

23-Jun-03 Release date: 08-Jun-04

Protein chain

O26773  (Y677_METTH) -  Uncharacterized protein MTH_677

Seq: 91 a.a.

Struc: 91 a.a.

DOI no: 10.1110/ps.04620504

Protein Sci 13:1458-1465 (2004)

PubMed id: 15152082

Solution structure of the hypothetical protein Mth677 from Methanobacterium thermoautotrophicum: a novel alpha+beta fold.

F.J.Blanco, A.Yee, R.Campos-Olivas, A.R.Ortiz, D.Devos, A.Valencia, C.H.Arrowsmith, M.Rico.

ABSTRACT

The structure of Mth677, a hypothetical protein from Methanobacterium thermoautotrophicum (Mth), has been determined by using heteronuclear nuclear magnetic resonance (NMR) methods on a double-labeled (15)N-(13)C sample. Mth677 adopts a novel alpha+beta fold, consisting of two alpha-helices (one N terminal and one C terminal) packed on the same side of a central beta-hairpin. This structure is likely shared by its three orthologs, detected in three other Archaebacteria. There are no clear features in the sequences of these proteins or in the genome organization of Mth to make a reliable functional assignment to this protein. However, the structural similarity to Escherichia coli MinE, the protein which controls that division occurs at the midcell site, lends support to the proposal that Mth677 might be, in Mth, the counterpart of the topological specificity domain of MinE in E. coli.

Selected figure(s)

Figure 3.
Figure 3. Stereo views of the solution structure of Mth677. (Top) Superposition (N, C^ , C^') of the 30 nuclear magnetic resonance (NMR) conformers showing the backbone in dark green, the hydrophobic core in pale green, the basic side chains in dark blue, the acidic ones in red, and the rest in cyan. (Bottom) View of Mth677 along its longitudinal axis where the predominantly acidic exterior of the protein can be seen. The figure was prepared with the program MolMol (Koradi et al. 1996).

Figure 7.
Figure 7. One bond 1H-15N single quantum correlation of nuclei 1H and 15N in Mt677 with assignments.

The above figures are reprinted by permission from the Protein Society: Protein Sci (2004, 13, 1458-1465) copyright 2004.

Figures were selected by an automated process.