6jv1: Difference between revisions
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==Crystal Structure of N-terminal domain of ArgZ, C264S mutant, bound to Substrate, an arginine dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria== | |||
<StructureSection load='6jv1' size='340' side='right'caption='[[6jv1]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jv1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JV1 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]] 1.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARG:ARGININE'>ARG</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=6jv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jv1 OCA], [https://pdbe.org/6jv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jv1 RCSB], [https://www.ebi.ac.uk/pdbsum/6jv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jv1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P74535_SYNY3 P74535_SYNY3] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A recently discovered ornithine-ammonia cycle (OAC) serves as a conduit in the nitrogen storage-and-remobilization machinery in cyanobacteria. The OAC involves an arginine-catabolic reaction catalyzed by the arginine dihydrolase ArgZ whose catalytic mechanism is unknown. Here, we determined the crystal structures at 1.2-3.0 A of unliganded ArgZ from the cyanobacterium Synechocystis sp. PCC6803 and of ArgZ complexed with its substrate arginine, a covalently linked reaction intermediate, or the reaction product ornithine. The structures reveal that a key residue, Asn(71), in the ArgZ active center, functions as the determinant distinguishing ArgZ from other members of the guanidino group-modifying enzyme superfamily. The structures, along with biochemical evidence from enzymatic assays coupled with electrospray ionization MS (ESI-MS) techniques, further suggest that ArgZ-catalyzed conversion of arginine to ornithine, ammonia, and carbon dioxide by ArgZ consists of two successive cycles of amine hydrolysis. Finally, we show that arginine dihydrolases are broadly distributed among bacteria and metazoan, suggesting that the OAC may be frequently used for redistribution of nitrogen from arginine catabolism or nitrogen fixation. | |||
Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond-rotation" catalytic mechanism.,Zhuang N, Zhang H, Li L, Wu X, Yang C, Zhang Y J Biol Chem. 2019 Dec 30. pii: RA119.011752. doi: 10.1074/jbc.RA119.011752. PMID:31914412<ref>PMID:31914412</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6jv1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] | |||
[[Category: Li L]] | |||
[[Category: Wu X]] | |||
[[Category: Zhang Y]] | |||
[[Category: Zhuang N]] | |||
Latest revision as of 13:20, 22 November 2023
Crystal Structure of N-terminal domain of ArgZ, C264S mutant, bound to Substrate, an arginine dihydrolase from the Ornithine-Ammonia Cycle in CyanobacteriaCrystal Structure of N-terminal domain of ArgZ, C264S mutant, bound to Substrate, an arginine dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria
Structural highlights
FunctionPublication Abstract from PubMedA recently discovered ornithine-ammonia cycle (OAC) serves as a conduit in the nitrogen storage-and-remobilization machinery in cyanobacteria. The OAC involves an arginine-catabolic reaction catalyzed by the arginine dihydrolase ArgZ whose catalytic mechanism is unknown. Here, we determined the crystal structures at 1.2-3.0 A of unliganded ArgZ from the cyanobacterium Synechocystis sp. PCC6803 and of ArgZ complexed with its substrate arginine, a covalently linked reaction intermediate, or the reaction product ornithine. The structures reveal that a key residue, Asn(71), in the ArgZ active center, functions as the determinant distinguishing ArgZ from other members of the guanidino group-modifying enzyme superfamily. The structures, along with biochemical evidence from enzymatic assays coupled with electrospray ionization MS (ESI-MS) techniques, further suggest that ArgZ-catalyzed conversion of arginine to ornithine, ammonia, and carbon dioxide by ArgZ consists of two successive cycles of amine hydrolysis. Finally, we show that arginine dihydrolases are broadly distributed among bacteria and metazoan, suggesting that the OAC may be frequently used for redistribution of nitrogen from arginine catabolism or nitrogen fixation. Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond-rotation" catalytic mechanism.,Zhuang N, Zhang H, Li L, Wu X, Yang C, Zhang Y J Biol Chem. 2019 Dec 30. pii: RA119.011752. doi: 10.1074/jbc.RA119.011752. PMID:31914412[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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