1ve6

From Proteopedia

(Difference between revisions)

Revision as of 13:21, 13 October 2021

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1

Structural highlights

1ve6 is a 2 chain structure with sequence from Aerpx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1ve7
Activity:	Acylaminoacyl-peptidase, with EC number 3.4.19.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[APEH_AERPE] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus.

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

Acylpeptide hydrolases (APH; also known as acylamino acid releasing enzyme) catalyze the removal of an N-acylated amino acid from blocked peptides. The crystal structure of an APH from the thermophilic archaeon Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a member of the prolyl oligopeptidase family of serine proteases. The structure of apAPH is a symmetric homodimer with each subunit comprised of two domains. The N-terminal domain is a regular seven-bladed beta-propeller, while the C-terminal domain has a canonical alpha/beta hydrolase fold and includes the active site and a conserved Ser445-Asp524-His556 catalytic triad. The complex structure of apAPH with an organophosphorus substrate, p-nitrophenyl phosphate, has also been determined. The complex structure unambiguously maps out the substrate binding pocket and provides a basis for substrate recognition by apAPH. A conserved mechanism for protein degradation from archaea to mammals is suggested by the structural features of apAPH.

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1.,Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z Structure. 2004 Aug;12(8):1481-8. PMID:15296741^[1]

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

References

↑ Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z. Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1. Structure. 2004 Aug;12(8):1481-8. PMID:15296741 doi:10.1016/j.str.2004.05.019

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ve6"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ve6' size='340' side='right'caption='[[1ve6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ve6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VE6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ve6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VE6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ve7|1ve7]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ve7|1ve7]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></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=1ve6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve6 OCA], [http://pdbe.org/1ve6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ve6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ve6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ve6 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=1ve6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve6 OCA], [https://pdbe.org/1ve6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ve6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ve6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ve6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/APEH_AERPE APEH_AERPE]] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus.
+[[https://www.uniprot.org/uniprot/APEH_AERPE APEH_AERPE]] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ve6

From Proteopedia

Revision as of 13:21, 13 October 2021

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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