PDBsum entry 3eas

Hydrolase

PDB id

3eas

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Contents

			Protein chains

					206 a.a. *

* Residue conservation analysis

PDB id:

3eas

Links

Name:

Hydrolase

Title:

Novel dimerization motif in the dead box RNA helicase hera: form 1, complete dimer, asymmetric

Structure:

Hera. Chain: a, b. Fragment: internal fragment (unp residues 215 to 426). Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 262724. Strain: hb27. Gene: tt_c1895. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.80Å

R-factor:

0.232

R-free:

0.314

Authors:

D.Klostermeier,M.G.Rudolph

Key ref:

D.Klostermeier and M.G.Rudolph (2009). A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility. Nucleic Acids Res, 37, 421-430. PubMed id: 19050012

Date:

26-Aug-08

Release date:

09-Dec-08

PROCHECK

	Headers

	References

Protein chains

Q72GF3 (Q72GF3_THET2) - Heat resistant RNA dependent ATPase from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

Seq: Struc:					517 a.a. 206 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	Nucleic Acids Res 37:421-430 (2009)
PubMed id: 19050012

A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
D.Klostermeier, M.G.Rudolph.

ABSTRACT

DEAD box helicases are involved in nearly all aspects of RNA metabolism. They share a common helicase core, and may comprise additional domains that contribute to RNA binding. The Thermus thermophilus helicase Hera is the first dimeric DEAD box helicase. Crystal structures of Hera fragments reveal a bipartite C-terminal domain with a novel dimerization motif and an RNA-binding module. We provide a first glimpse on the additional RNA-binding module outside the Hera helicase core. The dimerization and RNA-binding domains are connected to the C-terminal RecA domain by a hinge region that confers exceptional flexibility onto the helicase, allowing for different juxtapositions of the RecA-domains in the dimer. Combination of the previously determined N-terminal Hera structure with the C-terminal Hera structures allows generation of a model for the entire Hera dimer, where two helicase cores can work in conjunction on large RNA substrates.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20813532

E.Jankowsky (2011).
RNA helicases at work: binding and rearranging.

Trends Biochem Sci, 36, 19-29.

21391900

J.Strohmeier, I.Hertel, U.Diederichsen, M.G.Rudolph, and D.Klostermeier (2011).
Changing nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loop.

Biol Chem, 392, 357-369.

PDB codes:

3mwj 3mwk 3mwl 3nbf 3nej

19710183

M.G.Rudolph, and D.Klostermeier (2009).
The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core.

RNA, 15, 1993-2001.

PDB codes:

3i31 3i32

19747077

M.Hilbert, A.R.Karow, and D.Klostermeier (2009).
The mechanism of ATP-dependent RNA unwinding by DEAD box proteins.

Biol Chem, 390, 1237-1250.

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 codes are shown on the right.