9jet: Difference between revisions

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'''Unreleased structure'''


The entry 9jet is ON HOLD  until Paper Publication
==Crystal structure of a cupin protein (tm1459) in manganese (Mn) substituted form==
<StructureSection load='9jet' size='340' side='right'caption='[[9jet]], [[Resolution|resolution]] 1.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jet]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JET 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]] 1.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</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=9jet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jet OCA], [https://pdbe.org/9jet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jet RCSB], [https://www.ebi.ac.uk/pdbsum/9jet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jet ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X1H0_THEMA Q9X1H0_THEMA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The TM1459 protein from Thermotoga maritima is a member of the cupin protein superfamily and contains a mononuclear metal center. Structural information has been obtained using X-ray crystallography; however, its physiological role remains unknown. The metal-binding site has an octahedral coordination geometry ligated by four histidine imidazoles and two terminal water molecules present in the cis position. This protein had the ability to bind Mn, Fe, and Zn ions; additionally, a self-hydroxylation reaction occurred in the Fe-TM1459 C106V mutant. Namely, one of the tyrosine residues (Tyr7) was hydroxylated to generate the green form. Spectroscopic analyses using Vis-NIR, MALDI-TOF/MS, and resonance Raman spectroscopy confirmed that Tyr7 was hydroxylated to 3,4-dihydroxyphenylalanine giving an iron-catecholate complex. Because the Y7A/C106V mutant did not produce this green form, the mutation of Cys106 to Val was assumed to have induced a conformational change in Tyr7 that facilitated its approach to the metal center promoting the self-hydroxylation reaction. Thus, these results demonstrated that Fe-TM1459 protein has monooxygenase activity.


Authors:  
Unusual Self-Hydroxylation in 4-Histidine Tetrad-Supporting Nonheme Iron Center.,Fujieda N, Ishihama KI, Ichihashi H, Yanagisawa S, Kurisu G, Itoh S Chem Asian J. 2025 Apr 22:e202401191. doi: 10.1002/asia.202401191. PMID:40260495<ref>PMID:40260495</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9jet" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Fujieda N]]
[[Category: Ichihashi H]]
[[Category: Itoh S]]
[[Category: Kurisu G]]

Latest revision as of 18:07, 7 May 2025

Crystal structure of a cupin protein (tm1459) in manganese (Mn) substituted form

9jet, resolution 1.19Å

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