Dating agent prov4 7 1

An unusual α/β barrel consisting of eight α-helices (α4–α11) and eight β-strands (β2-β5, β8, β12–β14) forms the larger domain of the enzyme.

dating agent prov4 7 1-51

This data can be used to study global, correlated motions in atomic simulations of proteins.

Isocitrate lyase (ICL), one of the key enzymes of glyoxylate shunt, catalyzes the transformation of isocitrate to succinate and glyoxylate.

A similar feature has been reported in other proteins that help to form stable dimers Structure of Mtb ICL.

(A) Ribbon structure of the homotetrameric Mtb ICL, with each subunit shown in different color (PDB ID: 1F8I). Alterations in amino acid sequence could affect the native 3D conformation of the protein structure and to estimate the conformational modifications, MD simulations can be used for an in-depth analysis.

The small β-domain consisting of a short five-stranded β-sheet (β6, β7, β9–β11) and several of the active site residues lies on top of the α/β barrel.

One remarkable characteristic of this structure is the inter-subunit helix swapping of α12 and α13 between two non-crystallographically related subunits that are responsible for the tetrameric structure.

Isocitrate lyase (ICL), a potential anti-tubercular drug target, catalyzes the first step of the glyoxylate shunt.

In the present investigation, we studied the conformational flexibility of Mtb ICL to better understand its stability and catalytic activity.

The crystal structures of Mtb ICL are available in both apo-form and as complex with substrate analogues and inhibitors.

Mtb ICL is a tetrameric protein with each monomer containing 428 amino acids (Fig. Each subunit of Mtb ICL is composed of 14 α-helices and 14 β-strands.

To obtain a detailed description and understanding of the function of a protein, the 3D structure and an accurate description of its dynamics are therefore required.

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