6jv0: Difference between revisions

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<StructureSection load='6jv0' size='340' side='right'caption='[[6jv0]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
<StructureSection load='6jv0' size='340' side='right'caption='[[6jv0]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6jv0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JV0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JV0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6jv0]] 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=6JV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JV0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene></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]] 1.14&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sll1336 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jv0 OCA], [http://pdbe.org/6jv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jv0 RCSB], [http://www.ebi.ac.uk/pdbsum/6jv0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jv0 ProSAT]</span></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=6jv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jv0 OCA], [https://pdbe.org/6jv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jv0 RCSB], [https://www.ebi.ac.uk/pdbsum/6jv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jv0 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/P74535_SYNY3 P74535_SYNY3]
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jv0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Syny3]]
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
[[Category: Li, L]]
[[Category: Li L]]
[[Category: Wu, X]]
[[Category: Wu X]]
[[Category: Zhang, Y]]
[[Category: Zhang Y]]
[[Category: Zhuang, N]]
[[Category: Zhuang N]]
[[Category: Alpha/beta propeller fold]]
[[Category: Amidino-transferase domain]]
[[Category: Arginine dihydrolase]]
[[Category: Hydrolase]]

Latest revision as of 13:39, 27 March 2024

Crystal Structure of N-terminal domain of ArgZ, bound to Product, an arginine dihydrolase from the Ornithine-Ammonia Cycle in CyanobacteriaCrystal Structure of N-terminal domain of ArgZ, bound to Product, an arginine dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria

Structural highlights

6jv0 is a 1 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.14Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

P74535_SYNY3

6jv0, resolution 1.14Å

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OCA