Three-dimensional structure of a thermophilic family GH11 xylanase from Thermobifida fusca

Alicia Lammerts van Bueren1, Suzie Otani, Esben P Friis

  • 1Structural Biology Laboratory, Department of Chemistry, University of York, York, England.

Related Concept Videos

Hyperthermophilic Bacteria01:21

Hyperthermophilic Bacteria

Domain Bacteria includes some unique hyperthermophilic species. They exhibit remarkable adaptations that enable survival in extreme environments.Thermotoga species are rod-shaped, gram-negative, non-sporulating hyperthermophiles that form a sheath-like envelope called a toga. They ferment sugars or starch, producing lactate, acetate, CO₂, and H₂, and can also grow via anaerobic respiration using H₂ and ferric iron. Found in hot springs and hydrothermal vents, over 20% of their genes show strong...
Diversity of Archaea IV01:29

Diversity of Archaea IV

Hyperthermophilic archaea are a group of extremophiles thriving at temperatures above 80°C, often in hydrothermal vents and volcanic soils where conditions surpass the boiling point of water. At such temperatures, proteins, membranes, and DNA in most organisms degrade, but hyperthermophiles have evolved remarkable adaptations to maintain stability and function.Unique Cellular FeaturesHyperthermophilic membranes are composed of a monolayer of biphytanyl tetraether lipids, which resist thermal...
Diversity of Archaea III01:27

Diversity of Archaea III

Crenarchaeota, a prominent phylum of Archaea, is remarkable for its ability to thrive in extreme environments characterized by high temperatures and acidity. These microorganisms inhabit sulfuric hot springs, volcanic systems, and submarine hydrothermal vents, where temperatures often exceed 100°C. The unique adaptations of Crenarchaeota not only allow survival under such extreme conditions but also provide insights into the mechanisms of life in primordial Earth-like environments.Morphological...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...