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==Structural insights into novel mechanisms of inhibition of the major b-carbonic anhydrase CafB from the pathogenic fungus Aspergillus fumigatus (C116 flipped form)==
==Structural insights into novel mechanisms of inhibition of the major b-carbonic anhydrase CafB from the pathogenic fungus Aspergillus fumigatus (C116 flipped form)==
<StructureSection load='7cxw' size='340' side='right'caption='[[7cxw]]' scene=''>
<StructureSection load='7cxw' size='340' side='right'caption='[[7cxw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CXW FirstGlance]. <br>
<table><tr><td colspan='2'>[[7cxw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CXW FirstGlance]. <br>
</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=7cxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cxw OCA], [https://pdbe.org/7cxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cxw RCSB], [https://www.ebi.ac.uk/pdbsum/7cxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cxw ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=7cxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cxw OCA], [https://pdbe.org/7cxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cxw RCSB], [https://www.ebi.ac.uk/pdbsum/7cxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cxw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4DA32_ASPFU A4DA32_ASPFU] Reversible hydration of carbon dioxide.[RuleBase:RU003956]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In fungi the beta-class of carbonic anhydrases (beta-CAs) are zinc metalloenzymes that are essential for growth, survival, differentiation, and virulence. Aspergillus fumigatus is the most important pathogen responsible for invasive aspergillosis and possesses two major beta-CAs, CafA and CafB. Recently we reported the biochemical characterization and 1.8 A crystal structure of CafA. Here, we report a crystallographic analysis of CafB revealing the mechanism of enzyme catalysis and establish the relationship of this enzyme to other beta-CAs. While CafA has a typical open conformation, CafB, when exposed to acidic pH and/or an oxidative environment, has a novel type of active site in which a disulfide bond is formed between two zinc-ligating cysteines, expelling the zinc ion and stabilizing the inactive form of the enzyme. Based on the structural data, we generated an oxidation-resistant mutant (Y159A) of CafB. The crystal structure of the mutant under reducing conditions retains a catalytic zinc at the expected position, tetrahedrally coordinated by three residues (C57, H113 and C116) and an aspartic acid (D59), and replacing the zinc-bound water molecule in the closed form. Furthermore, the active site of CafB crystals grown under zinc-limiting conditions has a novel conformation in which the solvent-exposed catalytic cysteine (C116) is flipped out of the metal coordination sphere, facilitating release of the zinc ion. Taken together, our results suggest that A. fumigatus use sophisticated activity-inhibiting strategies to enhance its survival during infection.
Structural insights into novel mechanisms of inhibition of the major beta-carbonic anhydrase CafB from the pathogenic fungus Aspergillus fumigatus.,Kim S, Yeon J, Sung J, Kim NJ, Hong S, Jin MS J Struct Biol. 2021 Mar;213(1):107700. doi: 10.1016/j.jsb.2021.107700. Epub 2021 , Feb 3. PMID:33545350<ref>PMID:33545350</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cxw" style="background-color:#fffaf0;"></div>
==See Also==
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspergillus fumigatus Af293]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hong S]]
[[Category: Hong S]]
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