3ndv: Difference between revisions
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<StructureSection load='3ndv' size='340' side='right'caption='[[3ndv]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3ndv' size='340' side='right'caption='[[3ndv]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ndv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ndv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingosinicella_xenopeptidilytica Sphingosinicella xenopeptidilytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NDV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIC:(2S,5R,6R)-6-{[(2R)-2-AMINO-2-PHENYLETHANOYL]AMINO}-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC+ACID'>AIC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDV:(2S,4S)-2-[(1R)-1-{[(2R)-2-AMINO-2-PHENYLACETYL]AMINO}-2-OXOETHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>NDV</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIC:(2S,5R,6R)-6-{[(2R)-2-AMINO-2-PHENYLETHANOYL]AMINO}-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC+ACID'>AIC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDV:(2S,4S)-2-[(1R)-1-{[(2R)-2-AMINO-2-PHENYLACETYL]AMINO}-2-OXOETHYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>NDV</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=3ndv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ndv OCA], [https://pdbe.org/3ndv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ndv RCSB], [https://www.ebi.ac.uk/pdbsum/3ndv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ndv 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=3ndv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ndv OCA], [https://pdbe.org/3ndv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ndv RCSB], [https://www.ebi.ac.uk/pdbsum/3ndv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ndv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BAPA_SPHXN BAPA_SPHXN] Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.<ref>PMID:16109932</ref> <ref>PMID:17064315</ref> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Geueke | [[Category: Sphingosinicella xenopeptidilytica]] | ||
[[Category: Gruetter | [[Category: Geueke B]] | ||
[[Category: Heck | [[Category: Gruetter MG]] | ||
[[Category: Kohler | [[Category: Heck T]] | ||
[[Category: Merz | [[Category: Kohler H-PE]] | ||
[[Category: Merz T]] | |||
Latest revision as of 12:13, 6 September 2023
Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with ampicillinCrystal structure of the N-terminal beta-aminopeptidase BapA in complex with ampicillin
Structural highlights
FunctionBAPA_SPHXN Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.[1] [2] See AlsoReferences
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