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Related Concept Videos

Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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...
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...
Metal-Ligand Bonds02:51

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...

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Related Experiment Video

Updated: May 7, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Protoglobin: structure and ligand-binding properties.

Alessandra Pesce1, Martino Bolognesi, Marco Nardini

  • 1Department of Physics, University of Genova, Genova, Italy.

Advances in Microbial Physiology
|September 24, 2013
PubMed
Summary
This summary is machine-generated.

Protoglobin, the first archaeal globin, features a unique structure with two ligand access tunnels. Its function remains unknown, despite reversible O2, CO, and NO binding.

Keywords:
Archaea globinsDiatomic ligand recognitionGlobin foldGlobin-coupled sensorsHaem/ligand tunnelHaemoglobinHaemoglobin evolutionMyoglobinProtoglobin

More Related Videos

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

Related Experiment Videos

Last Updated: May 7, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

Area of Science:

  • Biochemistry
  • Structural Biology
  • Archaea Biology

Background:

  • Protoglobin is the first identified globin in Archaea, with an unknown biological role.
  • It exhibits reversible binding of O2, CO, and NO in vitro.
  • Archaean globins share a phylogenetic origin with globin-coupled sensor proteins.

Purpose of the Study:

  • To elucidate the unique structural features of Methanosarcina acetivorans protoglobin.
  • To understand the implications of its structure on ligand binding and function.
  • To provide insights into structure-function relationships within the globin superfamily.

Main Methods:

  • X-ray crystallography of Methanosarcina acetivorans protoglobin.
  • Analysis of tertiary and quaternary structures.
  • Investigation of ligand access tunnels and haem moiety accessibility.

Main Results:

  • Protoglobin possesses an expanded globin fold with a pre-A helix (Z) and N-terminal extension.
  • The haem moiety is deeply buried, accessed via two orthogonal tunnels (B/G and B/E helices).
  • Protoglobin forms a tight dimer via a four-helix bundle (G and H helices).

Conclusions:

  • Protoglobin exhibits unique structural adaptations, including a buried haem and a novel two-tunnel system.
  • Its low O2 dissociation rate and O2/CO selectivity favor O2 ligation.
  • Despite structural insights, the precise biological function of protoglobin remains to be determined and is a key area for future research.