1fy2

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(New page: 200px<br /><applet load="1fy2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fy2, resolution 1.2&Aring;" /> '''ASPARTYL DIPEPTIDASE'...)
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[[Image:1fy2.jpg|left|200px]]<br /><applet load="1fy2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fy2, resolution 1.2&Aring;" />
 
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'''ASPARTYL DIPEPTIDASE'''<br />
 
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==Overview==
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==Aspartyl Dipeptidase==
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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.
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<StructureSection load='1fy2' size='340' side='right'caption='[[1fy2]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fy2]] 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=1FY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FY2 FirstGlance]. <br>
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1FY2 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 CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA].
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</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>
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<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>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fy2 OCA], [https://pdbe.org/1fy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fy2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fy2 ProSAT]</span></td></tr>
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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]
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</table>
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[[Category: Salmonella typhimurium]]
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== Function ==
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[[Category: Single protein]]
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[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]
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[[Category: Hakansson, K.]]
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== Evolutionary Conservation ==
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[[Category: Miller, C.G.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Wang, A.H.J.]]
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Check<jmol>
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[[Category: CD]]
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<jmolCheckbox>
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[[Category: catalytic triad]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fy2_consurf.spt"</scriptWhenChecked>
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[[Category: peptidase]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: serine protease]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: strand-helix motif]]
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</jmolCheckbox>
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</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=1fy2 ConSurf].
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:27:15 2007''
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Hakansson K]]
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[[Category: Miller CG]]
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[[Category: Wang AH-J]]

Current revision

Aspartyl Dipeptidase

PDB ID 1fy2

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