View source for 4yu5


==Crystal structure of selenomethionine variant of Bacillus anthracis immune inhibitor A2 peptidase zymogen==
<StructureSection load='4yu5' size='340' side='right'caption='[[4yu5]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yu5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_biovar_anthracis_str._CI Bacillus cereus biovar anthracis str. CI]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YU5 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=KH2:3-(1-METHYLPIPERIDINIUM-1-YL)PROPANE-1-SULFONATE'>KH2</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4yu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu5 OCA], [https://pdbe.org/4yu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yu5 RCSB], [https://www.ebi.ac.uk/pdbsum/4yu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu5 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Immune inhibitor A(InhA)-type metallopeptidases are potential virulence factors secreted by members of the Bacillus cereus group. Two paralogs from anthrax-causing Bacillus anthracis (BaInhA1 and BaInhA2) were shown to degrade host tissue proteins with broad substrate specificity. Analysis of their activation mechanism and the crystal structure of a zymogenic BaInhA2 variant revealed a approximately 750-residue four-domain structure featuring a pro-peptide, a catalytic domain, a domain reminiscent of viral envelope glycoproteins, and a MAM domain grafted into the latter. This domain, previously found only in eukaryotes, is required for proper protein expression in B. anthracis and evinces certain flexibility. Latency is uniquely modulated by the N-terminal segment of the pro-peptide, which binds the catalytic zinc through its alpha-amino group and occupies the primed side of the active-site cleft. The present results further our understanding of the modus operandi of an anthrax secretome regulator.

Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome.,Arolas JL, Goulas T, Pomerantsev AP, Leppla SH, Gomis-Ruth FX Structure. 2016 Jan 5;24(1):25-36. doi: 10.1016/j.str.2015.10.015. PMID:26745529<ref>PMID:26745529</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Bacillus cereus biovar anthracis str. CI]]
[[Category: Large Structures]]
[[Category: Arolas JL]]
[[Category: Gomis-Ruth FX]]
[[Category: Goulas T]]