Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Residues Leu52 and Leu134 are important for the structural integrity of a nucleotide exchange factor GrpE from Bacillus licheniformis.

International journal of biological macromolecules - 1 Nov 2009

Liang Wan-Chi, Lin Min-Guan, Chou Wei-Mou, Chi Meng-Chun, Chang Hui-Ping, Lin Long-Liu

Abstract excerpt

A DNA fragment encoding Bacillus licheniformis GrpE (BlGrpE) with double mutations at codons 52 and 134 was obtained during PCR cloning. Leu52 and Leu134 in BlGrpE were individually replaced with Pro and His to generate BlGrpE-L52P and BlGrpE-L134H. BlGrpE and BlGrpE-L52P synergistically stimulat...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacillus
Share to Biophysical Phenomena
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Leucine

Share to Protein Denaturation

Share to Protein Renaturation

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 19665474
DOI: 10.1016/j.ijbiomac.2009.07.011

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19665474-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Residues Leu52 and Leu134 are important for the structural integrity of a nucleotide exchange factor GrpE from Bacillus licheniformis.PMID 19665474Read ↗

Site-saturation mutagenesis of leucine 134 of Bacillus licheniformis nucleotide exchange factor GrpE reveals the importance of this residue to the co-chaperone activity.Semantic proximity Read ↗

Spo0A can efficiently enhance the expression of the alkaline protease gene aprE in Bacillus licheniformis by specifically binding to its regulatory region.Semantic proximity Read ↗

Clamp-loader-helicase interaction in Bacillus. Leucine 381 is critical for pentamerization and helicase binding of the Bacillus tau protein.Semantic proximity Read ↗

Structural insights into the signal transduction mechanism of the K+-sensing two-component system KdpDE.Semantic proximity Read ↗

Improvement of the acid stability of Bacillus licheniformis alpha amylase by error-prone PCR.Semantic proximity Read ↗

GrpE N-terminal domain contributes to the interaction with Dnak and modulates the dynamics of the chaperone substrate binding domain.Semantic proximity Read ↗

Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations.Semantic proximity Read ↗

Mutation of leucine 20 causes a change of local conformation indirectly impairing the DNA binding of SP_0782 from Streptococcus pneumoniae.Semantic proximity Read ↗

Identification of the nucleotide exchange factor BmGrpE and its role under high-temperature stress in silkworm, Bombyx mori.Semantic proximity Read ↗

Mutational analysis of the nucleoid-associated protein HBsu of Bacillus subtilis.Semantic proximity Read ↗

Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: dimer dissociation by disruption of Val-Leu knot.Semantic proximity Read ↗

Modeling and monitoring the effects of three partly conserved Ile residues in the dimerization domain of a Mip-like virulence factor from Escherichia coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.