View source for 3zfo


==Crystal structure of substrate-like, unprocessed N-terminal protease Npro mutant S169P==
<StructureSection load='3zfo' size='340' side='right'caption='[[3zfo]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zfo]] is a 1 chain structure with sequence from [https://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=3ZFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZFO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=SGM:MONOTHIOGLYCEROL'>SGM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zfo OCA], [https://pdbe.org/3zfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zfo RCSB], [https://www.ebi.ac.uk/pdbsum/3zfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zfo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5L4B1_9FLAV Q5L4B1_9FLAV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Npro 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<ref>PMID:23643950</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zfo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pestivirus strain D32/00_HoBi]]
[[Category: Auer B]]
[[Category: Brandstetter H]]
[[Category: Koll M]]
[[Category: Schindler S]]
[[Category: Schneider R]]
[[Category: Sponring M]]
[[Category: Zogg T]]