PDBsum entry: 2asx

Unknown function

PDB id: 2asx

Contents

Protein chains

56 a.a. *

* Residue conservation analysis

Superseded by:

2l7h

PDB id:

2asx

Name:

Unknown function

Title:

The solution structure of the hamp domain of the hypothetica transmembrane receptor af1503

Structure:

Hypothetical protein af1503. Chain: a, b. Fragment: hamp domain. Engineered: yes

Source:

Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: af1503. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

22 models

Authors:

M.Coles,V.Truffault,M.Hulko,J.Martin,A.N.Lupas

Key ref:

M.Inouye (2006). Signaling by transmembrane proteins shifts gears. Cell, 126, 829-831. PubMed id: 16959559 DOI: 10.1016/j.cell.2006.08.024

Date:

24-Aug-05 Release date: 29-Aug-06

Protein chains

O28769  (O28769_ARCFU) -  Putative uncharacterized protein

Seq: 338 a.a.

Struc: 56 a.a.*

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

 Gene Ontology (GO) functional annotation 

• Cellular component: integral to membrane (1 term)
• Biological process: signal transduction (1 term)
• Biochemical function: signal transducer activity (1 term)

DOI no: 10.1016/j.cell.2006.08.024

Cell 126:829-831 (2006)

PubMed id: 16959559

Signaling by transmembrane proteins shifts gears.

M.Inouye.

ABSTRACT

The HAMP domain is present in a large number of transmembrane proteins in prokaryotes including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. In this issue of Cell, Hulko et al. (2006) report the NMR structure of a HAMP domain and present data suggesting that it transduces signals through a simple rotation of its four-helix parallel coiled coil.

Selected figure(s)

Figure 1.
Figure 1. Structure of the HAMP Domain
(Left) A histidine kinase is depicted based upon the Taz1 chimeric protein (Utsumi et al., 1989). The HAMP domain of the protein is illustrated as described in Hulko et al. (2006). The α2 helix of the HAMP domain is directly connected to the N-terminal helix of the EnvZ domain (DHp), forming a long single-helical rod (II^*). According to the findings of Hulko et al. (2006), the rotation of the α2 helix would simultaneously rotate the II^* helix, changing the relative configuration between the active-site histidine residue (H) and the ATP binding domain (CA). These relative positional changes may result in regulation of the histidine kinase activity.
(Right) Side chains of residues involved in packing interactions within the core of the domain are shown in red (x-layer geometry, in which side chains point straight at the center) and blue (da-layer geometry, in which side chains point away from the center). A cogwheel diagram corresponding to the top view is shown in which two packing modes are interconvertible by rotating adjacent helices by 26° in opposite directions.

The above figure is reprinted by permission from Cell Press: Cell (2006, 126, 829-831) copyright 2006.