|
|
Line 3: |
Line 3: |
| <StructureSection load='5tzb' size='340' side='right'caption='[[5tzb]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='5tzb' size='340' side='right'caption='[[5tzb]], [[Resolution|resolution]] 1.98Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5tzb]] is a 8 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TZB FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.977Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VK92_01140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1628208 Burkholderia sp. LK4])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tzb OCA], [http://pdbe.org/5tzb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tzb RCSB], [http://www.ebi.ac.uk/pdbsum/5tzb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tzb ProSAT]</span></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> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
Line 24: |
Line 24: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Burkholderia sp. lk4]] | + | [[Category: Burkholderia sp. LK4]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Drinkwater, N]] | + | [[Category: Drinkwater N]] |
- | [[Category: Dumsday, G]] | + | [[Category: Dumsday G]] |
- | [[Category: John, M]] | + | [[Category: John M]] |
- | [[Category: McGowan, S]] | + | [[Category: McGowan S]] |
- | [[Category: Beta-amino acid]]
| + | |
- | [[Category: Beta-aminopeptidase]]
| + | |
- | [[Category: Burkholderia]]
| + | |
- | [[Category: Enzyme]]
| + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Ntn hydrolase]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ John-White M, Dumsday GJ, Johanesen P, Lyras D, Drinkwater N, McGowan S. Crystal structure of a beta-aminopeptidase from an Australian Burkholderia sp. Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):386-392. doi:, 10.1107/S2053230X17007737. Epub 2017 Jun 17. PMID:28695846 doi:http://dx.doi.org/10.1107/S2053230X17007737
|