View source for 5nnb


==Isatin hydrolase A (IHA) from Labrenzia aggregata with isatinate bound==
<StructureSection load='5nnb' size='340' side='right'caption='[[5nnb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nnb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Roseibium_aggregatum Roseibium aggregatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NNB 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=92K:Isatinic+acid'>92K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5nnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nnb OCA], [https://pdbe.org/5nnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nnb RCSB], [https://www.ebi.ac.uk/pdbsum/5nnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nnb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0P0F0_ROSAI A0P0F0_ROSAI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catalytic mechanism of the cyclic amidohydrolase isatin hydrolase depends on a catalytically active manganese in the substrate-binding pocket. The Mn(2+) ion is bound by a motif also present in other metal dependent hydrolases like the bacterial kynurenine formamidase. The crystal structures of the isatin hydrolases from Labrenzia aggregata and Ralstonia solanacearum combined with activity assays allow for the identification of key determinants specific for the reaction mechanism. Active site residues central to the hydrolytic mechanism include a novel catalytic triad Asp-His-His supported by structural comparison and hybrid quantum mechanics/classical mechanics simulations. A hydrolytic mechanism for a Mn(2+) dependent amidohydrolases that disfavour Zn(2+) as the primary catalytically active site metal proposed here is supported by these likely cases of convergent evolution. The work illustrates a fundamental difference in the substrate-binding mode between Mn(2+) dependent isatin hydrolase like enzymes in comparison with the vast number of Zn(2+) dependent enzymes.

A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase.,Sommer T, Bjerregaard-Andersen K, Uribe L, Etzerodt M, Diezemann G, Gauss J, Cascella M, Morth JP Sci Rep. 2018 Aug 30;8(1):13104. doi: 10.1038/s41598-018-31259-y. PMID:30166577<ref>PMID:30166577</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nnb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Roseibium aggregatum]]
[[Category: Bjerregaard-Andersen K]]
[[Category: Morth JP]]
[[Category: Sommer T]]