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[[Image:1fye.gif|left|200px]]


{{Structure
==Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)==
|PDB= 1fye |SIZE=350|CAPTION= <scene name='initialview01'>1fye</scene>, resolution 1.20&Aring;
<StructureSection load='1fye' size='340' side='right'caption='[[1fye]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=[[1fy2|1FY2]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fye OCA], [http://www.ebi.ac.uk/pdbsum/1fye PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fye RCSB]</span>
== Function ==
}}
[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]
 
== Evolutionary Conservation ==
'''ASPARTYL DIPEPTIDASE (ANISOTROPIC B-FACTOR REFINEMENT)'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fye_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1FYE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYE OCA].  
</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].
 
<div style="clear:both"></div>
==Reference==
__TOC__
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://www.ncbi.nlm.nih.gov/pubmed/11106384 11106384]
</StructureSection>
[[Category: Salmonella typhimurium]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Hakansson, K.]]
[[Category: Hakansson K]]
[[Category: Miller, C G.]]
[[Category: Miller CG]]
[[Category: Wang, A H.J.]]
[[Category: Wang AH-J]]
[[Category: catalytic triad]]
[[Category: peptidase]]
[[Category: serine protease]]
[[Category: strand-helix motif]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:32:39 2008''

Latest revision as of 07:20, 7 February 2024

Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)

1fye, resolution 1.20Å

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