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Frontier of Protein Crystallography II

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: closed (1 May 2022) | Viewed by 8225

Special Issue Editor

CEB Centre of Excellence in Biocrystallography, Department of Chemical and Pharmaceutical Sciences, University of Trieste, Trieste, Italy
Interests: crystallography; structural biology; Vitamin B12 proteins; redox-proteins; drug delivery; diagnostics; metals in medicine; bioinorganic chemistry; supramolecular chemistry; nanostructures
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein crystallography continues to develop vigorously and today there are over 120,000 structures deposited at the Protein Data Bank (PDB), 90% of which are from X-ray data. The technological developments behind this rapid growth involve all crucial steps of the pipeline “from gene to structure”: from the developments of wet lab technologies, including recombinant DNA techniques, protein purification, and crystallization; to innovative hardware technology, for example, brilliant light sources such as synchrotrons and X-ray free-electron lasers (XFEL) together with high-frame-rate and ultra-sensitive detectors. An important impetus to protein crystallography has also been provided by soft technology: theoretical foundations, computational algorithms, and software development. The bio-crystallography integrated with cryo-electron microscopy is a major research trend in structural biology.

Our First volume is successful and attracts a lot of attention. This research field is still full of possibilities. This Special Issue will focus on covering frontier technologies and methodologies in protein crystallography, as well as their novel applications.

Prof. Dr. Silvano Geremia
Guest Editor

Manuscript Submission Information

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Keywords

  • X-ray crystallography
  • recombinant protein overexpression
  • protein purification
  • protein crystallization
  • cryo-crystallography
  • radiation sources
  • X-ray detectors
  • structural biology software
  • high-throughput crystallography
  • structural biology

Published Papers (1 paper)

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Review

18 pages, 27561 KiB  
Review
Structural Diversity of Ubiquitin E3 Ligase
by Sachiko Toma-Fukai and Toshiyuki Shimizu
Molecules 2021, 26(21), 6682; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26216682 - 04 Nov 2021
Cited by 45 | Viewed by 7842
Abstract
The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating [...] Read more.
The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases. Full article
(This article belongs to the Special Issue Frontier of Protein Crystallography II)
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