2qzp: Difference between revisions
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<StructureSection load='2qzp' size='340' side='right'caption='[[2qzp]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2qzp' size='340' side='right'caption='[[2qzp]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2qzp]] 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=2QZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QZP FirstGlance]. <br> | ||
</td></tr><tr id=' | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qzp OCA], [https://pdbe.org/2qzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qzp RCSB], [https://www.ebi.ac.uk/pdbsum/2qzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qzp 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=2qzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qzp OCA], [https://pdbe.org/2qzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qzp RCSB], [https://www.ebi.ac.uk/pdbsum/2qzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qzp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2qzp ConSurf]. | </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=2qzp ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Acylpeptide hydrolase (APH) catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids. The crystal structure of recombinant APH from the thermophilic archaeon Aeropyrum pernix K1 (apAPH) was reported recently to be at a resolution of 2.1 Angstrom; using X-ray diffraction. A truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal, apAPH-delta(1-21), was cloned, expressed, characterized and crystallized. Data from biochemical experiments indicate that the optimum temperature of apAPH is decreased by 15 degrees C with the deletion of the N-terminal alpha-helix. However, the enzyme activity at the optimal temperature does not change. It suggests that this N-terminal alpha-helix is essential for thermostability. Here, the crystal structure of apAPH-delta(1-21) has been determined by molecular replacement to 2.5 Angstrom;. A comparison between the two structures suggests a difference in thermostability, and it can be concluded that by adding or deleting a linking structure (located over different domains), the stability or even the activity of an enzyme can be modified. | |||
Expression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1.,Zhang HF, Zheng BS, Peng Y, Lou ZY, Feng Y, Rao ZH Acta Biochim Biophys Sin (Shanghai). 2005 Sep;37(9):613-7. doi: , 10.1111/j.1745-7270.2005.00085.x. PMID:16143816<ref>PMID:16143816</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2qzp" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]] | *[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aeropyrum pernix]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rao | [[Category: Rao Z]] | ||
[[Category: Zhang | [[Category: Zhang HF]] | ||
[[Category: Zheng | [[Category: Zheng BS]] | ||
