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The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Cycloheptatriene is a neutral monocyclic unsaturated hydrocarbon that consists of an odd number of carbon atoms and an intervening sp3 carbon in the ring. The three double bonds in the ring correspond to 6 π electrons, which is a Huckel number, and therefore satisfies the criteria of 4n + 2 π electrons. However, the intervening sp3 carbon disrupts the continuous overlap of p orbitals. As a result, cycloheptatriene is not aromatic.
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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.
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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Published on: July 16, 2017

Acyl carrier protein structural classification and normal mode analysis.

David C Cantu1, Michael J Forrester, Katherine Charov

  • 1Department of Chemical and Biological Engineering, Iowa State University, Ames, Iowa 50011, USA.

Protein Science : a Publication of the Protein Society
|March 1, 2012
PubMed
Summary
This summary is machine-generated.

Acyl carrier proteins (ACPs) were classified into 16 families based on sequence and structure. This analysis reveals evolutionary relationships and dynamic properties of ACPs, aiding in understanding their biological functions.

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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Acyl carrier proteins (ACPs) are essential components of fatty acid and polyketide biosynthesis.
  • Understanding the structural diversity and evolutionary relationships of ACPs is crucial for elucidating their diverse biological roles.

Purpose of the Study:

  • To create a comprehensive database (ThYme) of ACP structures.
  • To classify ACPs based on sequence and structural similarity.
  • To investigate the evolutionary origins and dynamic properties of ACPs.

Main Methods:

  • Data mining of primary and tertiary structures from existing databases.
  • Sequence similarity analysis for classification into families.
  • Tertiary structure superposition for validation.
  • Normal mode analysis of freestanding structures.
  • Prediction of tertiary structures for uncharacterized ACP families.

Main Results:

  • The ThYme database was established, containing all known ACP structures.
  • ACPs were classified into 16 distinct families with statistically significant sequence differences.
  • Structural superposition supported these classifications, revealing high similarity within certain families, suggesting common ancestry.
  • Normal mode analysis indicated higher flexibility at termini and loops compared to helices.
  • Intra-family mode overlap was greater than inter-family overlap, reinforcing family distinctions.
  • Tertiary structures were successfully predicted for three previously uncharacterized ACP families.

Conclusions:

  • The classification of ACPs into 16 families provides a robust framework for studying their structure-function relationships.
  • Evidence suggests a common evolutionary origin for several ACP families.
  • Dynamic analysis highlights conserved flexible regions within ACPs, potentially important for their function.
  • The prediction of novel ACP structures expands the known structural repertoire and aids future research.