View source for 5tzb


==Burkholderia sp. beta-aminopeptidase==
<StructureSection load='5tzb' size='340' side='right'caption='[[5tzb]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tzb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_sp._LK4 Burkholderia sp. LK4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TZB 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]] 1.977&#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></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=5tzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tzb OCA], [https://pdbe.org/5tzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tzb RCSB], [https://www.ebi.ac.uk/pdbsum/5tzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tzb ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
beta-Aminopeptidases are a unique group of enzymes that have the unusual capability to hydrolyze N-terminal beta-amino acids from synthetic beta-peptides. beta-Peptides can form secondary structures mimicking alpha-peptide-like structures that are resistant to degradation by most known proteases and peptidases. These characteristics of beta-peptides give them great potential as peptidomimetics. Here, the X-ray crystal structure of BcA5-BapA, a beta-aminopeptidase from a Gram-negative Burkholderia sp. that was isolated from activated sludge from a wastewater-treatment plant in Australia, is reported. The crystal structure of BcA5-BapA was determined to a resolution of 2.0 A and showed a tetrameric assembly typical of the beta-aminopeptidases. Each monomer consists of an alpha-subunit (residues 1-238) and a beta-subunit (residues 239-367). Comparison of the structure of BcA5-BapA with those of other known beta-aminopeptidases shows a highly conserved structure and suggests a similar proteolytic mechanism of action.

Crystal structure of a beta-aminopeptidase from an Australian Burkholderia sp.,John-White M, Dumsday GJ, Johanesen P, Lyras D, Drinkwater N, McGowan S Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):386-392. doi:, 10.1107/S2053230X17007737. Epub 2017 Jun 17. PMID:28695846<ref>PMID:28695846</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5tzb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia sp. LK4]]
[[Category: Large Structures]]
[[Category: Drinkwater N]]
[[Category: Dumsday G]]
[[Category: John M]]
[[Category: McGowan S]]