Sandbox Reserved 1068

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Introduction

Mycobacterim tuberculosis salicylate synthase (MtbI) is a highly promiscuous enzyme that has four distinct activities: isochorismate synthase (IS), isochorismate pyruvate lyase (IPL), salicylate synthase (SS) and chromate mutate (CM).

Structure

The crystal asymmetric unit was found to contain four MbtI molecules, however crystal packing and size exclusion chromatography data suggest a monomeric enzyme. There are no significant structural changes between the four monomers excepts from the localized differences in the active site. The overall molecular structure consist of a polypeptide of 450 residues that forms one large single domain with a similar fold to other chromate-utilizing enzymes. The fold consists of two alpha/deta subdomains, each forming a large antiparallel beta sheet with helices packed around the outside of the two beta sheets that form the core.

Function

Disease

The salicylate synthase activity of MbtI produces salicylate from chorismate through an isochorismate intermediate. This reaction is Mg dependent. Chorismate is then used in the biosyntheses of Mycobactin T, the siderophore of M. tuberculosis. The siderophore sequesters iron, covering pathogenesis of M. tuberculosis.

Relevance

Structural highlights

Inhibition Studies

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.