3n33: Difference between revisions

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<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=3n33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n33 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n33 RCSB], [http://www.ebi.ac.uk/pdbsum/3n33 PDBsum]</span></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=3n33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n33 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n33 RCSB], [http://www.ebi.ac.uk/pdbsum/3n33 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q52VH2_9SPHN Q52VH2_9SPHN]] 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==
*[[Aminopeptidase|Aminopeptidase]]
*[[Aminopeptidase|Aminopeptidase]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

Revision as of 16:48, 25 December 2014

Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with pefabloc SC (AEBSF)Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with pefabloc SC (AEBSF)

Structural highlights

3n33 is a 4 chain structure with sequence from Sphingosinicella xenopeptidilytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:bapA (Sphingosinicella xenopeptidilytica)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[Q52VH2_9SPHN] 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 Also

References

  1. Geueke B, Namoto K, Seebach D, Kohler HP. A novel beta-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic beta-tri- and beta-dipeptides. J Bacteriol. 2005 Sep;187(17):5910-7. PMID:16109932 doi:http://dx.doi.org/187/17/5910
  2. Geueke B, Heck T, Limbach M, Nesatyy V, Seebach D, Kohler HP. Bacterial beta-peptidyl aminopeptidases with unique substrate specificities for beta-oligopeptides and mixed beta,alpha-oligopeptides. FEBS J. 2006 Dec;273(23):5261-72. Epub 2006 Oct 25. PMID:17064315 doi:http://dx.doi.org/10.1111/j.1742-4658.2006.05519.x

3n33, resolution 1.80Å

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