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| | <StructureSection load='1ve7' size='340' side='right'caption='[[1ve7]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1ve7' size='340' side='right'caption='[[1ve7]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ve7]] 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=1VE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VE7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ve7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VE7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ve6|1ve6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ve7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve7 OCA], [https://pdbe.org/1ve7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ve7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ve7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ve7 ProSAT]</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=1ve7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve7 OCA], [http://pdbe.org/1ve7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ve7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ve7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ve7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acylaminoacyl-peptidase]] | + | [[Category: Aeropyrum pernix]] |
| - | [[Category: Aerpx]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bartlam, M]] | + | [[Category: Bartlam M]] |
| - | [[Category: Cao, S]] | + | [[Category: Cao S]] |
| - | [[Category: Feng, Y]] | + | [[Category: Feng Y]] |
| - | [[Category: Gao, R]] | + | [[Category: Gao R]] |
| - | [[Category: Rao, Z]] | + | [[Category: Rao Z]] |
| - | [[Category: Wang, G]] | + | [[Category: Wang G]] |
| - | [[Category: Xie, G]] | + | [[Category: Xie G]] |
| - | [[Category: Yang, H]] | + | [[Category: Yang H]] |
| - | [[Category: Zhao, X]] | + | [[Category: Zhao X]] |
| - | [[Category: Alpha/beta hydrolase domain]]
| + | |
| - | [[Category: Beta propeller domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
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.
See Also
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
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