7wgi: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of AflSQS from Aspergillus flavus== | |||
<StructureSection load='7wgi' size='340' side='right'caption='[[7wgi]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7wgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WGI FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IND:INDOLE'>IND</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7wgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wgi OCA], [https://pdbe.org/7wgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wgi RCSB], [https://www.ebi.ac.uk/pdbsum/7wgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wgi ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A364LX79_ASPFL A0A364LX79_ASPFL] Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene.[RuleBase:RU368088] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
There is interest in the development of drugs to treat fungal infections due to the increasing threat of drug resistance, and here, we report the first crystallographic structure of the catalytic domain of a fungal squalene synthase (SQS), Aspergillus flavus SQS (AfSQS), a potential drug target, together with a bioinformatics study of fungal, human, and protozoal SQSs. Our X-ray results show strong structural similarities between the catalytic domains in these proteins, but, remarkably, using bioinformatics, we find that there is also a large, highly polar helix in the fungal proteins that connects the catalytic and membrane-anchoring transmembrane domains. This polar helix is absent in squalene synthases from all other lifeforms. We show that the transmembrane domain in AfSQS and in other SQSs, stannin, and steryl sulfatase, have very similar properties (% polar residues, hydrophobicity, and hydrophobic moment) to those found in the "penultimate" C-terminal helical domain in squalene epoxidase, while the final C-terminal domain in squalene epoxidase is more polar and may be monotopic. We also propose structural models for full-length AfSQS based on the bioinformatics results as well as a deep learning program that indicate that the C-terminus region may also be membrane surface-associated. Taken together, our results are of general interest given the unique nature of the polar helical domain in fungi that may be involved in protein-protein interactions as well as being a future target for antifungals. | |||
A Structural and Bioinformatics Investigation of a Fungal Squalene Synthase and Comparisons with Other Membrane Proteins.,Malwal SR, Shang N, Liu W, Li X, Zhang L, Chen CC, Guo RT, Oldfield E ACS Omega. 2022 Jun 17;7(26):22601-22612. doi: 10.1021/acsomega.2c01924., eCollection 2022 Jul 5. PMID:35811857<ref>PMID:35811857</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7wgi" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspergillus flavus]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen CC]] | |||
[[Category: Guo RT]] | |||
[[Category: Liu WD]] | |||
[[Category: Shang N]] | |||