1fye

From Proteopedia

(Difference between revisions)

Revision as of 05:46, 28 April 2021

Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)

Structural highlights

1fye is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1fy2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hakansson K, Wang AH, Miller CG. The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:11106384 doi:10.1073/pnas.260376797

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fye"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fye' size='340' side='right'caption='[[1fye]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fye]] is a 1 chain structure. 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>
+<table><tr><td colspan='2'>[[1fye]] is a 1 chain structure. 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>
-</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>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fy2|1fy2]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fy2|1fy2]]</div></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=1fye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fye OCA], [http://pdbe.org/1fye PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fye RCSB], [http://www.ebi.ac.uk/pdbsum/1fye PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fye ProSAT]</span></td></tr>
+<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>
 </table>
 == Function ==
-[[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]
+[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1fye

From Proteopedia

Revision as of 05:46, 28 April 2021

Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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