View source for 7esr


==Crystal structure of Synechocystis sp PCC6803 guanidinium hydrolase (R32)==
<StructureSection load='7esr' size='340' side='right'caption='[[7esr]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7esr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ESR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ESR 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]] 1.42&#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>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=7esr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7esr OCA], [https://pdbe.org/7esr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7esr RCSB], [https://www.ebi.ac.uk/pdbsum/7esr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7esr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPEB2_SYNY3 SPEB2_SYNY3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nitrogen availability is a growth-limiting factor in many habitats(1), and the global nitrogen cycle involves prokaryotes and eukaryotes competing for this precious resource. Only some bacteria and archaea can fix elementary nitrogen; all other organisms depend on the assimilation of mineral or organic nitrogen. The nitrogen-rich compound guanidine occurs widely in nature(2-4), but its utilization is impeded by pronounced resonance stabilization(5), and enzymes catalysing hydrolysis of free guanidine have not been identified. Here we describe the arginase family protein GdmH (Sll1077) from Synechocystis sp. PCC 6803 as a Ni(2+)-dependent guanidine hydrolase. GdmH is highly specific for free guanidine. Its activity depends on two accessory proteins that load Ni(2+) instead of the typical Mn(2+) ions into the active site. Crystal structures of GdmH show coordination of the dinuclear metal cluster in a geometry typical for arginase family enzymes and allow modelling of the bound substrate. A unique amino-terminal extension and a tryptophan residue narrow the substrate-binding pocket and identify homologous proteins in further cyanobacteria, several other bacterial taxa and heterokont algae as probable guanidine hydrolases. This broad distribution suggests notable ecological relevance of guanidine hydrolysis in aquatic habitats.

Discovery of a Ni(2+)-dependent guanidine hydrolase in bacteria.,Funck D, Sinn M, Fleming JR, Stanoppi M, Dietrich J, Lopez-Igual R, Mayans O, Hartig JS Nature. 2022 Mar;603(7901):515-521. doi: 10.1038/s41586-022-04490-x. Epub 2022, Mar 9. PMID:35264792<ref>PMID:35264792</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7esr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Fleming JR]]
[[Category: Mayans OM]]