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1fye

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[[Image:1fye.png|left|200px]]
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==Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)==
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<StructureSection load='1fye' size='340' side='right' caption='[[1fye]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fye]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYE FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fy2|1fy2]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1fye RCSB], [http://www.ebi.ac.uk/pdbsum/1fye PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fye_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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{{STRUCTURE_1fye| PDB=1fye | SCENE= }}
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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:11106384<ref>PMID:11106384</ref>
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===Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_11106384}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1fye]] is a 1 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:011106384</ref><references group="xtra"/>
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Hakansson, K.]]
[[Category: Hakansson, K.]]

Revision as of 12:39, 28 September 2014

Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)

1fye, resolution 1.20Å

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