PDBsum entry 2h2m

Metal transport

PDB id: 2h2m

Contents

Protein chain

108 a.a. *

* Residue conservation analysis

PDB id:

2h2m

Name:

Metal transport

Title:

Solution structure of the n-terminal domain of commd1 (murr1)

Structure:

Comm domain-containing protein 1. Chain: a. Synonym: protein murr1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: commd1. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

M.Sommerhalter,Y.Zhang,A.C.Rosenzweig

Key ref:

M.Sommerhalter et al. (2007). Solution structure of the COMMD1 N-terminal domain. J Mol Biol, 365, 715-721. PubMed id: 17097678 DOI: 10.1016/j.jmb.2006.10.030

Date:

19-May-06 Release date: 05-Dec-06

Protein chain

Q8N668  (COMD1_HUMAN) -  COMM domain-containing protein 1 from Homo sapiens

Seq: 190 a.a.

Struc: 108 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2006.10.030

J Mol Biol 365:715-721 (2007)

PubMed id: 17097678

Solution structure of the COMMD1 N-terminal domain.

M.Sommerhalter, Y.Zhang, A.C.Rosenzweig.

ABSTRACT

COMMD1 is the prototype of a new protein family that plays a role in several important cellular processes, including NF-kappaB signaling, sodium transport, and copper metabolism. The COMMD proteins interact with one another via a conserved C-terminal domain, whereas distinct functions are predicted to result from a variable N-terminal domain. The COMMD proteins have not been characterized biochemically or structurally. Here, we present the solution structure of the N-terminal domain of COMMD1 (N-COMMD1, residues 1-108). This domain adopts an alpha-helical structure that bears little resemblance to any other helical protein. The compact nature of N-COMMD1 suggests that full-length COMMD proteins are modular, consistent with specific functional properties for each domain. Interactions between N-COMMD1 and partner proteins may occur via complementary electrostatic surfaces. These data provide a new foundation for biochemical characterization of COMMD proteins and for probing COMMD1 protein-protein interactions at the molecular level.

Selected figure(s)

Figure 1.
Figure 1. Stereoview of the 20 conformers representing the solution structure of N-COMMD1. The well-ordered regions comprise residues 9–19 and 30–101. Figure 1. Stereoview of the 20 conformers representing the solution structure of N-COMMD1. The well-ordered regions comprise residues 9–19 and 30–101.

Figure 2.
Figure 2. Ribbon diagram of the averaged and energy minimized structure of N-COMMD1 generated with PyMOL [http://pymol.sourceforge.net/]. The N-terminus is colored in blue and the C-terminus in red. Figure 2. Ribbon diagram of the averaged and energy minimized structure of N-COMMD1 generated with PyMOL [http://pymol.sourceforge.net/]. The N-terminus is colored in blue and the C-terminus in red.

The above figures are reprinted from an Open Access publication published by Elsevier: J Mol Biol (2007, 365, 715-721) copyright 2007.

Figures were selected by an automated process.