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==Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12== | |||
<StructureSection load='5cnx' size='340' side='right' caption='[[5cnx]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cnx]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CNX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CNX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cnx OCA], [http://pdbe.org/5cnx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cnx RCSB], [http://www.ebi.ac.uk/pdbsum/5cnx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cnx ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/YPDF_ECOLI YPDF_ECOLI]] Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine.<ref>PMID:15901689</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Are, V]] | [[Category: Are, V]] | ||
[[Category: | [[Category: Ghosh, B]] | ||
[[Category: Jamdar, S]] | |||
[[Category: Kumar, A]] | [[Category: Kumar, A]] | ||
[[Category: | [[Category: Makde, R D]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: Pepq]] | |||
[[Category: Prolidase]] | |||
[[Category: Xaa-pro aminopeptidase]] |
Revision as of 18:29, 26 July 2016
Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12
Structural highlights
Function[YPDF_ECOLI] Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine.[1] References
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