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[[Image:1fye.gif|left|200px]]<br /><applet load="1fye" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fye, resolution 1.20&Aring;" />
'''ASPARTYL DIPEPTIDASE (ANISOTROPIC B-FACTOR REFINEMENT)'''<br />


==Overview==
==Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)==
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.
<StructureSection load='1fye' size='340' side='right'caption='[[1fye]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1fye]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FYE FirstGlance]. <br>
1FYE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYE OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fye OCA], [https://pdbe.org/1fye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fye RCSB], [https://www.ebi.ac.uk/pdbsum/1fye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fye ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106384 11106384]
</table>
[[Category: Salmonella typhimurium]]
== Function ==
[[Category: Single protein]]
[https://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]
[[Category: Hakansson, K.]]
== Evolutionary Conservation ==
[[Category: Miller, C G.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Wang, A H.J.]]
Check<jmol>
[[Category: CD]]
  <jmolCheckbox>
[[Category: catalytic triad]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fye_consurf.spt"</scriptWhenChecked>
[[Category: peptidase]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: serine protease]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: strand-helix motif]]
  </jmolCheckbox>
 
</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/main_output.php?pdb_ID=1fye ConSurf].
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:56 2008''
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Hakansson K]]
[[Category: Miller CG]]
[[Category: Wang AH-J]]

Latest revision as of 07:20, 7 February 2024

Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)

1fye, resolution 1.20Å

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