View source for 9cip


==MicroED structure of the C11 cysteine protease clostripain==
<StructureSection load='9cip' size='340' side='right'caption='[[9cip]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cip]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hathewaya_histolytica Hathewaya histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CIP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2.5&#8491;</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=9cip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cip OCA], [https://pdbe.org/9cip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cip RCSB], [https://www.ebi.ac.uk/pdbsum/9cip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cip ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CLOS_HATHI CLOS_HATHI] Cysteine endopeptidase with strict specificity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Clostripain secreted from Clostridium histolyticum is the founding member of the C11 family of Clan CD cysteine peptidases, which is an important group of peptidases secreted by numerous bacteria. Clostripain is an arginine-specific endopeptidase. Because of its efficacy as a cysteine peptidase, it is widely used in laboratory settings. Despite its importance the structure of clostripain remains unsolved. Here we describe the first structure of an active form of C. histolyticum clostripain determined at 2.5 A resolution using microcrystal electron diffraction (MicroED). The structure was determined from a single nanocrystal after focused ion beam milling. The structure of clostripain shows a typical Clan CD alpha/beta/alpha sandwich architecture and the Cys231/His176 catalytic dyad in the active site. It has a large electronegative substrate binding pocket showing its ability to accommodate large and diverse substrates. A loop in the heavy chain formed between residues 452 and 457 is potentially important for substrate binding. In conclusion, this result demonstrates the importance of MicroED to determine the unknown structure of macromolecules such as clostripain, which can be further used as a platform to study substrate binding and design of potential inhibitors against this class of peptidases.

MicroED structure of the C11 cysteine protease clostripain.,Ruma YN, Bu G, Hattne J, Gonen T J Struct Biol X. 2024 Jul 6;10:100107. doi: 10.1016/j.yjsbx.2024.100107. , eCollection 2024 Dec. PMID:39100863<ref>PMID:39100863</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cip" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hathewaya histolytica]]
[[Category: Large Structures]]
[[Category: Bu G]]
[[Category: Gonen T]]
[[Category: Hattne J]]
[[Category: Ruma YN]]