1fy2

<StructureSection load='1fy2' size='340' side='right' caption='[[1fy2]], [[Resolution|resolution]] 1.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1fy2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FY2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fye|1fye]]</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=1fy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fy2 OCA], [http://pdbe.org/1fy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fy2 RCSB], [http://www.ebi.ac.uk/pdbsum/1fy2 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/PEPE_SALTY PEPE_SALTY]] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fy2_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in alpha/beta-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity.

The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.,Hakansson K, Wang AH, Miller CG Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:11106384<ref>PMID:11106384</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1fy2" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hakansson, K]]

[[Category: Miller, C G]]

[[Category: Wang, A H.J]]

[[Category: Catalytic triad]]

[[Category: Hydrolase]]

[[Category: Peptidase]]

[[Category: Strand-helix motif]]