1ve6: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ve6]] is a 2 chain structure with 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=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 [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. 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> | ||
</td></tr><tr><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><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> | ||
<tr><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">[[1ve7|1ve7]]</td></tr> | ||
<tr><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'>[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><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://www.rcsb.org/pdb/explore.do?structureId=1ve6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ve6 PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=1ve6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ve6 PDBsum]</span></td></tr> | ||
<table> | </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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Acylaminoacyl-peptidase]] | [[Category: Acylaminoacyl-peptidase]] | ||
[[Category: Aeropyrum pernix]] | [[Category: Aeropyrum pernix]] | ||
[[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: Alpha/beta hydrolase domain]] | ||
[[Category: Beta propeller domain]] | [[Category: Beta propeller domain]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 16:34, 25 December 2014
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1
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 PubMedAcylpeptide 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 AlsoReferences
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