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[[Image:1ve7.gif|left|200px]]
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{{STRUCTURE_1ve7|  PDB=1ve7  |  SCENE=  }}
'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate'''


==Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate==
<StructureSection load='1ve7' size='340' side='right'caption='[[1ve7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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='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>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/1ve7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1ve7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:15296741</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1VE7 is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 1ve7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15296741 15296741]
*[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]]
[[Category: Acylaminoacyl-peptidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeropyrum pernix]]
[[Category: Aeropyrum pernix]]
[[Category: Single protein]]
[[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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:26:05 2008''

Latest revision as of 07:33, 30 October 2024

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate

1ve7, resolution 2.70Å

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