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Korostelev, Andrei

One or more keywords matched the following properties of Korostelev, Andrei

Property	Value
overview	Structure and Function of the Ribosome Visit Korostelev Lab Web Page Ribosomes, the ancient and universal cellular machines, are responsible for decoding genetic information and synthesizing proteins in all living organisms. A eubacterial ribosome has a molecular weight of approximately 2.5 MDa and consists of about 55 proteins and 3 large RNA molecules. So far, the ribosome is the largest asymmetric macromolecule amenable to crystallographic analyses. The multi-step process of translation is not fully understood: only recently, structural details of some steps of translation started to emerge. In our lab, we aim at a full structural description of the highly dynamic process of translation. We use X-ray crystallography to obtain snapshots of different functional states of the ribosome and biochemistry to test the hypotheses concerning the mechanisms and dynamics of the ribosome and translation factors. These studies are designed not only to expand our fundamental knowledge of this molecular machine but also to aid in the development of new drugs that target ribosomes. Translation termination on the 70S ribosome.Release factor RF2 (yellow) is bound to the ribosome in response to a stop codon encoded in a messenger RNA (green) located on the small 30S ribosomal subunit (cyan and blue). RF2 is positioned to catalyze the hydrolysis of a peptidyl-tRNA (green and orange) on the large 50S subunit (grey, purple and magenta). An E-site-bound tRNA is in red. This structural model was rendered in Pymol and is based on the X-ray structures of 70S translation termination complexes (Korostelev et al., 2008; Laurberg et al., 2008) and a 70S-tRNA complex (Jenner et al., 2010).
Rotation Projects	Rotation projects We apply X-ray crystallography and biochemical methods to understand the mechanisms employed by the ribosome. Potential rotation projects are 1) to understand various aspects of translation via mutagenesis/biochemical assays, 2) to crystallize and work on determining the structures of translation factors and functional ribosome complexes, and 3) to improve computational methods used to determine crystal structures of macromolecules. Feel free to contact the lab for a more detailed discussion.

Property

Value

overview

Structure and Function of the Ribosome

Visit Korostelev Lab Web Page

Ribosomes, the ancient and universal cellular machines, are responsible for decoding genetic information and synthesizing proteins in all living organisms. A eubacterial ribosome has a molecular weight of approximately 2.5 MDa and consists of about 55 proteins and 3 large RNA molecules. So far, the ribosome is the largest asymmetric macromolecule amenable to crystallographic analyses.

The multi-step process of translation is not fully understood: only recently, structural details of some steps of translation started to emerge.

In our lab, we aim at a full structural description of the highly dynamic process of translation. We use X-ray crystallography to obtain snapshots of different functional states of the ribosome and biochemistry to test the hypotheses concerning the mechanisms and dynamics of the ribosome and translation factors. These studies are designed not only to expand our fundamental knowledge of this molecular machine but also to aid in the development of new drugs that target ribosomes.

Translation termination on the 70S ribosome.Release factor RF2 (yellow) is bound to the ribosome in response to a stop codon encoded in a messenger RNA (green) located on the small 30S ribosomal subunit (cyan and blue). RF2 is positioned to catalyze the hydrolysis of a peptidyl-tRNA (green and orange) on the large 50S subunit (grey, purple and magenta). An E-site-bound tRNA is in red.

This structural model was rendered in Pymol and is based on the X-ray structures of 70S translation termination complexes (Korostelev et al., 2008; Laurberg et al., 2008) and a 70S-tRNA complex (Jenner et al., 2010).

Rotation Projects

Rotation projects

We apply X-ray crystallography and biochemical methods to understand the mechanisms employed by the ribosome. Potential rotation projects are 1) to understand various aspects of translation via mutagenesis/biochemical assays, 2) to crystallize and work on determining the structures of translation factors and functional ribosome complexes, and 3) to improve computational methods used to determine crystal structures of macromolecules.

Feel free to contact the lab for a more detailed discussion.

One or more keywords matched the following items that are connected to Korostelev, Andrei

Item Type	Name
Academic Article	Crystal structure of an RNA helix recognized by a zinc-finger protein: an 18-bp duplex at 1.6 A resolution.
Academic Article	Bias in cross-validated free R factors: mitigation of the effects of non-crystallographic symmetry.
Academic Article	Interactions and dynamics of the Shine Dalgarno helix in the 70S ribosome.
Academic Article	Structural basis for translation termination on the 70S ribosome.
Academic Article	Crystal structure of a translation termination complex formed with release factor RF2.
Academic Article	Crystal structure of the 70S ribosome bound with the Q253P mutant form of release factor RF2.
Academic Article	Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements.
Academic Article	Analysis of structural dynamics in the ribosome by TLS crystallographic refinement.
Academic Article	The unfolded protein response signals through high-order assembly of Ire1.
Academic Article	Multistart simulated annealing refinement of the crystal structure of the 70S ribosome.
Academic Article	Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1.
Academic Article	Crystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3.
Academic Article	Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome.
Concept	Crystallography, X-Ray
Academic Article	Initiation of translation in bacteria by a structured eukaryotic IRES RNA.
Academic Article	Mechanism of premature translation termination on a sense codon.

Search Criteria

Crystallography X Ray