7bop

<table><tr><td colspan='2'>[[7bop]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_A1163 Aspergillus fumigatus A1163]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BOP FirstGlance]. <br>

== Function ==

[https://www.uniprot.org/uniprot/B0Y2F5_ASPFC B0Y2F5_ASPFC]

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Fungal cell walls and their biosynthetic enzymes are potential targets for novel antifungal agents. Recently, two mannosyltransferases, namely core-mannan synthases A (CmsA/Ktr4) and B (CmsB/Ktr7), were found to play roles in the core-mannan biosynthesis of fungal-type galactomannan. CmsA/Ktr4 is an alpha-(1--&gt;2)-mannosyltransferase responsible for alpha-(1--&gt;2)-mannan biosynthesis in fungal-type galactomannan, which covers the cell surface of Aspergillus fumigatus Strains with disrupted cmsA/ktr4 have been shown to exhibit strongly suppressed hyphal elongation and conidiation alongside reduced virulence in a mouse model of invasive aspergillosis, indicating that CmsA/Ktr4 is a potential novel antifungal candidate. In this study we present the 3-D structures of the soluble catalytic domain of CmsA/Ktr4, as determined by X-ray crystallography at a resolution of 1.95A, as well as the enzyme and Mn(2+)/GDP complex to 1.90A resolution. The CmsA/Ktr4 protein not only contains a highly conserved binding pocket for the donor substrate, GDP-mannose, but also has a unique broad cleft structure formed by its N- and C-terminal regions and is expected to recognize the acceptor substrate, a mannan chain. Based on these crystal structures, we also present a 3-D structural model of the enzyme-substrate complex generated using docking and molecular dynamics simulations with alpha-Man-(1--&gt;6)-alpha-Man-(1--&gt;2)-alpha-Man-OMe as the model structure for the acceptor substrate. This predicted enzyme-substrate complex structure is also supported by findings from single amino acid substitution CmsA/Ktr4 mutants expressed in DeltacmsA/ktr4 A fumigatus cells. Taken together, these results provide basic information for developing specific alpha-mannan biosynthesis inhibitors for use as pharmaceuticals and/or pesticides.

Structural basis for the core-mannan biosynthesis of cell wall fungal-type galactomannan in Aspergillus fumigatus.,Hira D, Onoue T, Oka T J Biol Chem. 2020 Sep 1. pii: RA120.013742. doi: 10.1074/jbc.RA120.013742. PMID:32873705<ref>PMID:32873705</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 7bop" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Aspergillus fumigatus A1163]]