PPubMed6 Jul 2010Cited 36×

Structural classification of proteins and structural genomics: new insights into protein folding and evolution Structural classification of proteins

Antonina Andreeva, Alexey G. Murzin

Abstract

This review article surveys the protein structures determined by Joint Center for Structural Genomics and published in this special issue of Acta Crystallographica Section F.

A figure from Structural classification of proteins and structural genomics: new insights into protein folding and evolution Structural classification of proteins — fig. from the paper

§ The Valyu brief

The paper, in five minutes

Read from the full text via Valyu Contents

Structural genomics reveals new protein architectures, unusual topologies, and metamorphic folds, reshaping our understanding of protein evolution.

What’s new

i.Survey of JCSG‑determined protein structures published in Acta Cryst. F
ii.Identification of novel β‑sheet architectures such as double‑barrel and β‑spiral roll
iii.Discovery of unusual topologies including knotted proteins and metamorphic folds
iv.Insights into protein fold evolution and the impact of structural genomics on expanding fold space

How they did it

The authors compiled protein structures solved by the Joint Center for Structural Genomics and other SG efforts, focusing on those published in this issue. They analyzed the structures using SCOP classification, comparing folds, architectures, and topologies to identify novel and atypical features.

What they found

Determined three acetoacetate decarboxylase structures (PDB 3c8w, 3cmb, 3bh2) revealing a double‑barrel fold
Identified two DUF1285 structures (PDB 2re3, 2ra9) showing a duplicated consensus fold
Characterized two metamorphic DUF74 pentamer structures (PDB 1y2i, 1vr4) with subunits adopting different conformations
Found that more than one structural representative now exists for most characterized families, indicating extensive coverage of fold space

Caveats

✕Many newly identified folds lack functional annotation and await complementary biological data
✕The review relies on several unpublished structures, limiting independent verification
✕Discovery rate of completely novel folds has slowed, suggesting remaining fold space may be limited

§ The Valyu brief

Reading the full paper and taking notes. This takes a few seconds…

§ Ask this paper

Ask a question about this paper

Valyu reads the full text and answers from what the paper actually says.

§ Related work in other archives

Similar papers in all four archives

The same idea searched in arXiv, PubMed, bioRxiv and chemRxiv at once, so a method can lead you to where it is being applied.

AarXiv4 found

PPubMed4 found

BbioRxiv4 found

CchemRxiv4 found

Searching the other archives…