View source for 3woi


==Crystal structure of the DAP BII (S657A)==
<StructureSection load='3woi' size='340' side='right'caption='[[3woi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3woi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_700993 Atcc 700993]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WOI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3woj|3woj]], [[3wok|3wok]], [[3wol|3wol]], [[3wom|3wom]], [[3won|3won]], [[3woo|3woo]], [[3wop|3wop]], [[3woq|3woq]], [[3wor|3wor]]</div></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=3woi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3woi OCA], [https://pdbe.org/3woi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3woi RCSB], [https://www.ebi.ac.uk/pdbsum/3woi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3woi ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The dipeptidyl aminopeptidase BII (DAP BII) belongs to a serine peptidase family, S46. The amino acid sequence of the catalytic unit of DAP BII exhibits significant similarity to those of clan PA endopeptidases, such as chymotrypsin. However, the molecular mechanism of the exopeptidase activity of family S46 peptidase is unknown. Here, we report crystal structures of DAP BII. DAP BII contains a peptidase domain including a typical double beta-barrel fold and previously unreported alpha-helical domain. The structures of peptide complexes revealed that the alpha-helical domain covers the active-site cleft and the side chain of Asn330 in the domain forms hydrogen bonds with the N-terminus of the bound peptide. These observations indicate that the alpha-helical domain regulates the exopeptidase activity of DAP BII. Because S46 peptidases are not found in mammals, we expect that our study will be useful for the design of specific inhibitors of S46 peptidases from pathogens.

S46 peptidases are the first exopeptidases to be members of clan PA.,Sakamoto Y, Suzuki Y, Iizuka I, Tateoka C, Roppongi S, Fujimoto M, Inaka K, Tanaka H, Masaki M, Ohta K, Okada H, Nonaka T, Morikawa Y, Nakamura KT, Ogasawara W, Tanaka N Sci Rep. 2014 May 15;4:4977. doi: 10.1038/srep04977. PMID:24827749<ref>PMID:24827749</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3woi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 700993]]
[[Category: Large Structures]]
[[Category: Fujimoto, M]]
[[Category: Iizuka, I]]
[[Category: Nonaka, T]]
[[Category: Ogasawara, W]]
[[Category: Roppongi, S]]
[[Category: Sakamoto, Y]]
[[Category: Suzuki, Y]]
[[Category: Tanaka, N]]
[[Category: Tateoka, C]]
[[Category: Chymotrypsin fold]]
[[Category: Hydrolase]]
[[Category: S46 peptidase]]