PDBsum entry 2k0g

Membrane protein

PDB id

2k0g

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Contents

			Protein chain

					142 a.a. *

			Ligands

					CMP

* Residue conservation analysis

PDB id:

2k0g

Links

Name:

Membrane protein

Title:

Solution structure of a bacterial cyclic nucleotide-activated k+ channel binding domain in complex with camp

Structure:

Mll3241 protein. Chain: a. Fragment: cyclic nucleotide binding domain, residues 216-355. Engineered: yes

Source:

Rhizobium loti. Mesorhizobium loti. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

15 models

Authors:

S.Schunke,M.Stoldt,D.Willbold

Key ref:

S.Schünke et al. (2009). Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP. Embo Rep, 10, 729-735. PubMed id: 19465888

Date:

02-Feb-08

Release date:

10-Feb-09

PROCHECK

	Headers

	References

Protein chain

Q98GN8 (CNGK1_RHILO) - Cyclic nucleotide-gated potassium channel mll3241 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)

Seq: Struc:					355 a.a. 142 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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

	Embo Rep 10:729-735 (2009)
PubMed id: 19465888

Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP.
S.Schünke, M.Stoldt, K.Novak, U.B.Kaupp, D.Willbold.

ABSTRACT

Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are crucial in neuronal excitability and signal transduction of sensory cells. HCN and CNG channels are activated by binding of cyclic nucleotides to their intracellular cyclic nucleotide-binding domain (CNBD). However, the mechanism by which the binding of cyclic nucleotides opens these channels is not well understood. Here, we report the solution structure of the isolated CNBD of a cyclic nucleotide-sensitive K(+) channel from Mesorhizobium loti. The protein consists of a wide anti-parallel beta-roll topped by a helical bundle comprising five alpha-helices and a short 3(10)-helix. In contrast to the dimeric arrangement ('dimer-of-dimers') in the crystal structure, the solution structure clearly shows a monomeric fold. The monomeric structure of the CNBD supports the hypothesis that the CNBDs transmit the binding signal to the channel pore independently of each other.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20729090

A.Cukkemane, R.Seifert, and U.B.Kaupp (2011).
Cooperative and uncooperative cyclic-nucleotide-gated ion channels.

Trends Biochem Sci, 36, 55-64.

21430265

S.Schünke, M.Stoldt, J.Lecher, U.B.Kaupp, and D.Willbold (2011).
Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel.

Proc Natl Acad Sci U S A, 108, 6121-6126.

PDB code:

2kxl

21336931

T.Drepper, U.Krauss, S.Meyer Zu Berstenhorst, J.Pietruszka, and K.E.Jaeger (2011).
Lights on and action! Controlling microbial gene expression by light.

Appl Microbiol Biotechnol, 90, 23-40.

20449776

S.Schünke, J.Lecher, M.Stoldt, U.B.Kaupp, and D.Willbold (2010).
Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain.

Biomol NMR Assign, 4, 147-150.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.