4pf1: Difference between revisions
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New page: '''Unreleased structure''' The entry 4pf1 is ON HOLD Authors: Michalska, K., Chhor, G., Fayman, K., Endres, M., Jedrzejczak, R., Babnigg, G., Steen, A., Lloyd, K., Joachimiak, A., Midwe... |
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==Crystal structure of aminopeptidase from marine sediment archaeon Thaumarchaeota archaeon== | |||
<StructureSection load='4pf1' size='340' side='right'caption='[[4pf1]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4pf1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumarchaeota_archaeon_SCGC_AB-539-E09 Thaumarchaeota archaeon SCGC AB-539-E09]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PF1 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=4pf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pf1 OCA], [https://pdbe.org/4pf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pf1 RCSB], [https://www.ebi.ac.uk/pdbsum/4pf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pf1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/M7TVE7_9ARCH M7TVE7_9ARCH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Marine sediments host a large population of diverse, heterotrophic, uncultured microorganisms with unknown physiologies that control carbon flow through organic matter decomposition. Recently, single-cell genomics uncovered new key players in these processes, such as the miscellaneous crenarchaeotal group. These widespread archaea encode putative intra- and extracellular proteases for the degradation of detrital proteins present in sediments. Here, we show that one of these enzymes is a self-compartmentalizing tetrameric aminopeptidase with a preference for cysteine and hydrophobic residues at the N terminus of the hydrolyzed peptide. The ability to perform detailed characterizations of enzymes from native subsurface microorganisms, without requiring that those organisms first be grown in pure culture, holds great promise for understanding key carbon transformations in the environment as well as identifying new enzymes for biomedical and biotechnological applications. | |||
New aminopeptidase from "microbial dark matter" archaeon.,Michalska K, Steen AD, Chhor G, Endres M, Webber AT, Bird J, Lloyd KG, Joachimiak A FASEB J. 2015 Sep;29(9):4071-9. doi: 10.1096/fj.15-272906. Epub 2015 Jun 10. PMID:26062601<ref>PMID:26062601</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4pf1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thaumarchaeota archaeon SCGC AB-539-E09]] | |||
[[Category: Babnigg G]] | |||
[[Category: Chhor G]] | |||
[[Category: Endres M]] | |||
[[Category: Fayman K]] | |||
[[Category: Jedrzejczak R]] | |||
[[Category: Joachimiak A]] | |||
[[Category: Lloyd K]] | |||
[[Category: Michalska K]] | |||
[[Category: Steen A]] | |||
Latest revision as of 07:16, 27 September 2023
Crystal structure of aminopeptidase from marine sediment archaeon Thaumarchaeota archaeon
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