3zfp: Difference between revisions
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==Crystal structure of product-like, processed N-terminal protease Npro with internal His-Tag== | ==Crystal structure of product-like, processed N-terminal protease Npro with internal His-Tag== | ||
<StructureSection load='3zfp' size='340' side='right' caption='[[3zfp]], [[Resolution|resolution]] 1.25Å' scene=''> | <StructureSection load='3zfp' size='340' side='right'caption='[[3zfp]], [[Resolution|resolution]] 1.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zfp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pestivirus_strain_d32/00_hobi Pestivirus strain d32/00_hobi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZFP FirstGlance]. <br> | <table><tr><td colspan='2'>[[3zfp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pestivirus_strain_d32/00_hobi Pestivirus strain d32/00_hobi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZFP FirstGlance]. <br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pestivirus strain d32/00_hobi]] | [[Category: Pestivirus strain d32/00_hobi]] | ||
[[Category: Auer, B]] | [[Category: Auer, B]] |
Revision as of 14:46, 17 July 2019
Crystal structure of product-like, processed N-terminal protease Npro with internal His-TagCrystal structure of product-like, processed N-terminal protease Npro with internal His-Tag
Structural highlights
Publication Abstract from PubMedNpro is a key effector protein of pestiviruses such as bovine viral diarrhea virus and abolishes host cell antiviral defense mechanisms. Synthesized as the N-terminal part of the viral polyprotein, Npro releases itself via an autoproteolytic cleavage, triggering its immunological functions. However, the mechanisms of its proteolytic action and its immune escape were unclear. Here, we present the crystal structures of Npro to 1.25 A resolution. Structures of pre- and postcleavage intermediates identify three catalytically relevant elements. The trapping of the putative catalytic water reveals its distinct roles as a base, acid, and nucleophile. The presentation of the substrate further explains the enigmatic latency of the protease, ensuring a single in cis cleavage. Additionally, we identified a zinc-free, disulfide-linked conformation of the TRASH motif, an interaction hub of immune factors. The structure opens additional opportunities in utilizing Npro as an autocleaving fusion protein and as a pharmaceutical target. Crystal Structures of the Viral Protease Npro Imply Distinct Roles for the Catalytic Water in Catalysis.,Zogg T, Sponring M, Schindler S, Koll M, Schneider R, Brandstetter H, Auer B Structure. 2013 Apr 30. pii: S0969-2126(13)00112-3. doi:, 10.1016/j.str.2013.04.003. PMID:23643950[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Large Structures
- Pestivirus strain d32/00 hobi
- Auer, B
- Brandstetter, H
- Koll, M
- Schindler, S
- Schneider, R
- Sponring, M
- Zogg, T
- Auto-processing cysteine protease
- Auto-proteolysis
- Convergent evolution
- Host-pathogen interaction
- Hydrolase
- Hydroxide-dependent catalysis
- Immune modulation
- In cis- cleavage
- Pestivirus
- Viral protease