Related Experiment Video

Updated: Aug 12, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

Crystal structure of the anti-fungal target N-myristoyl transferase

S A Weston1, R Camble, J Colls

  • 1Zeneca Pharmaceuticals, Macclesfield, UK.

Nature Structural Biology
|March 21, 1998
PubMed

Insights

N-myristoyl transferase (NMT) is crucial for Candida albicans growth. Determining its structure aids in developing new antifungal drugs by targeting this essential enzyme.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Mycology

Background:

  • N-myristoyl transferase (NMT) catalyzes essential protein modification in eukaryotes.
  • Candida albicans NMT is vital for fungal growth and a target for antifungal drug development.
  • The enzyme exhibits no sequence homology to other proteins and possesses a unique alpha/beta fold.

Purpose of the Study:

  • To determine the structure of Candida albicans NMT.
  • To provide insights for the rational design of selective NMT inhibitors.
  • To facilitate the development of novel antifungal therapies.

Main Methods:

  • Protein structure determination (details not specified in abstract).

Main Results:

  • The NMT structure reveals a novel alpha/beta fold with internal two-fold symmetry.
  • A prominent groove and deep pocket were identified on the protein surface.
  • The pocket floor, characterized by negative charge and proximity to a conserved glutamic acid, is proposed as the catalytic center.

Conclusions:

  • The identified groove and pocket are suggested as substrate-binding sites.
  • The negatively charged pocket floor is implicated as the catalytic center of NMT.
  • Structural insights into C. albicans NMT can guide the development of targeted antifungal agents.

More Related Videos

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep105011:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip10:45

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Published on: March 20, 2021

Related Concept Videos

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Inhibitors of Gram-positive Cell Wall Synthesis01:23

Inhibitors of Gram-positive Cell Wall Synthesis

Bacterial cell walls are typically rigid structures composed mainly of peptidoglycan, a mesh-like polymer that provides mechanical strength and maintains cell shape. The synthesis of peptidoglycan is a crucial process in bacterial growth and serves as a primary target for many antibiotics.Mechanism of Action of Beta-Lactam AntibioticsBeta-lactam antibiotics, such as penicillin, inhibit peptidoglycan synthesis in actively growing cells. These antibiotics share a characteristic four-membered...
Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...
Antifungal Agents01:15

Antifungal Agents

Amphotericin B is a broad-spectrum antifungal agent that exploits structural differences between fungal and mammalian cell membranes. Its amphipathic structure—featuring a hydrophobic polyene-lactone ring and a hydrophilic region containing mycosamine and carboxylic acid groups—enables selective binding to ergosterol, a sterol predominantly found in fungal plasma membranes. This selective interaction underlies the drug’s antifungal activity, although weak binding to cholesterol contributes to...