PDBsum entry 3ffq

Metal transport

PDB id

3ffq

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Contents

			Protein chains

					184 a.a. *

			Metals

					_BR ×9

			Waters ×71

* Residue conservation analysis

PDB id:

3ffq

Links

Name:

Metal transport

Title:

Hcn2i 443-640 apo-state

Structure:

Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2. Chain: a, b. Synonym: brain cyclic nucleotide-gated channel 2, bcng-2, hyperpolarization-activated cation channel 1, hac-1. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: bcng2, bcng2 or hac1, hac1, hcn2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.40Å

R-factor:

0.245

R-free:

0.283

Authors:

N.B.Olivier

Key ref:

J.W.Taraska et al. (2009). Mapping the structure and conformational movements of proteins with transition metal ion FRET. Nat Methods, 6, 532-537. PubMed id: 19525958 DOI: 10.1038/nmeth.1341

Date:

04-Dec-08

Release date:

23-Jun-09

PROCHECK

	Headers

	References

Protein chains

O88703 (HCN2_MOUSE) - Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 from Mus musculus

Seq: Struc:

Seq: Struc:					863 a.a. 184 a.a.

Key:

Secondary structure

CATH domain

DOI no: 10.1038/nmeth.1341	Nat Methods 6:532-537 (2009)
PubMed id: 19525958

Mapping the structure and conformational movements of proteins with transition metal ion FRET.
J.W.Taraska, M.C.Puljung, N.B.Olivier, G.E.Flynn, W.N.Zagotta.

ABSTRACT

Visualizing conformational dynamics in proteins has been difficult, and the atomic-scale motions responsible for the behavior of most allosteric proteins are unknown. Here we report that fluorescence resonance energy transfer (FRET) between a small fluorescent dye and a nickel ion bound to a dihistidine motif can be used to monitor small structural rearrangements in proteins. This method provides several key advantages over classical FRET, including the ability to measure the dynamics of close-range interactions, the use of small probes with short linkers, a low orientation dependence, and the ability to add and remove unique tunable acceptors. We used this 'transition metal ion FRET' approach along with X-ray crystallography to determine the structural changes of the gating ring of the mouse hyperpolarization-activated cyclic nucleotide-regulated ion channel HCN2. Our results suggest a general model for the conformational switch in the cyclic nucleotide-binding site of cyclic nucleotide-regulated ion channels.

Literature references that cite this PDB file's key reference

PubMed id

Reference

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

20036207

C.Zhao, L.M.Hellman, X.Zhan, W.S.Bowman, S.W.Whiteheart, and M.G.Fried (2010).
Hexahistidine-tag-specific optical probes for analyses of proteins and their interactions.

Anal Biochem, 399, 237-245.

20434995

J.W.Taraska, and W.N.Zagotta (2010).
Fluorescence applications in molecular neurobiology.

Neuron, 66, 170-189.

19823671

J.D.Fessenden (2009).
Förster resonance energy transfer measurements of ryanodine receptor type 1 structure using a novel site-specific labeling method.

PLoS One, 4, e7338.

19805285

J.W.Taraska, M.C.Puljung, and W.N.Zagotta (2009).
Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions.

Proc Natl Acad Sci U S A, 106, 16227-16232.

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.