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1th5

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==Solution structure of C-terminal domain of NifU-like protein from Oryza sativa==
==Solution structure of C-terminal domain of NifU-like protein from Oryza sativa==
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<StructureSection load='1th5' size='340' side='right'caption='[[1th5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='1th5' size='340' side='right'caption='[[1th5]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1th5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Orysa Orysa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TH5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1th5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TH5 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q48|1q48]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1th5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1th5 OCA], [https://pdbe.org/1th5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1th5 RCSB], [https://www.ebi.ac.uk/pdbsum/1th5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1th5 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=1th5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1th5 OCA], [https://pdbe.org/1th5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1th5 RCSB], [https://www.ebi.ac.uk/pdbsum/1th5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1th5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NIFU1_ORYSJ NIFU1_ORYSJ]] Molecular scaffold for [Fe-S] cluster assembly of chloroplastic iron-sulfur proteins (By similarity).
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[https://www.uniprot.org/uniprot/NIFU1_ORYSJ NIFU1_ORYSJ] Molecular scaffold for [Fe-S] cluster assembly of chloroplastic iron-sulfur proteins (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1th5 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1th5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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NifU-like proteins are a highly conserved protein that serves as the scaffold for assembly of Fe-S clusters. Chloroplastic NifU-like proteins have tandem NifU like domains, named domain I and domain II. Although the amino acid sequences of these domains are very similar to each other, the predicted functional region for the Fe-S cluster assembly, the CXXC motif, exists only in domain I. The structure of the domain II of chloroplastic NifU-like protein OsNifU1A has an alpha-beta sandwich structure containing two alpha helices located on one side of the beta-sheet. The electrostatic surface potential of OsNifU1A domain II is predominantly positively charged. Chloroplastic NifU-like proteins are targeted to ferredoxin for transferring the Fe-S cluster. The ferredoxin presents an overall negatively charged surface, which may evoke an electrostatic association with OsNifU1A domain II.
 
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The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A.,Kumeta H, Ogura K, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F J Biomol NMR. 2007 Jun;38(2):161-4. Epub 2007 Apr 13. PMID:17431550<ref>PMID:17431550</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1th5" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Orysa]]
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[[Category: Oryza sativa]]
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[[Category: Asayama, M]]
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[[Category: Asayama M]]
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[[Category: Inagaki, F]]
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[[Category: Inagaki F]]
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[[Category: Katoh, E]]
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[[Category: Katoh E]]
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[[Category: Katoh, S]]
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[[Category: Katoh S]]
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[[Category: Kumeta, H]]
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[[Category: Kumeta H]]
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[[Category: Ogura, K]]
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[[Category: Ogura K]]
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[[Category: Iron-sulfur cluster binding]]
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[[Category: Program for rice genome research]]
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[[Category: Structural genomic]]
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[[Category: Unknown function]]
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Revision as of 08:41, 1 May 2024

Solution structure of C-terminal domain of NifU-like protein from Oryza sativa

PDB ID 1th5

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