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== | ==Structural genomics, protein ybgI, unknown function== | ||
<StructureSection load='1nmo' size='340' side='right'caption='[[1nmo]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nmo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NMO 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1nmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmo OCA], [https://pdbe.org/1nmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nmo RCSB], [https://www.ebi.ac.uk/pdbsum/1nmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GCH1L_ECOLI GCH1L_ECOLI] Provides significant protection from radiation damage and may be involved in the degradation of radiation-damaged nucleotides.<ref>PMID:25049088</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/1nmo_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1nmo ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BACKGROUND: The protein encoded by the gene ybgI was chosen as a target for a structural genomics project emphasizing the relation of protein structure to function. RESULTS: The structure of the ybgI protein is a toroid composed of six polypeptide chains forming a trimer of dimers. Each polypeptide chain binds two metal ions on the inside of the toroid. CONCLUSION: The toroidal structure is comparable to that of some proteins that are involved in DNA metabolism. The di-nuclear metal site could imply that the specific function of this protein is as a hydrolase-oxidase enzyme. | BACKGROUND: The protein encoded by the gene ybgI was chosen as a target for a structural genomics project emphasizing the relation of protein structure to function. RESULTS: The structure of the ybgI protein is a toroid composed of six polypeptide chains forming a trimer of dimers. Each polypeptide chain binds two metal ions on the inside of the toroid. CONCLUSION: The toroidal structure is comparable to that of some proteins that are involved in DNA metabolism. The di-nuclear metal site could imply that the specific function of this protein is as a hydrolase-oxidase enzyme. | ||
Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site.,Ladner JE, Obmolova G, Teplyakov A, Howard AJ, Khil PP, Camerini-Otero RD, Gilliland GL BMC Struct Biol. 2003 Sep 30;3:7. PMID:14519207<ref>PMID:14519207</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Escherichia coli | <div class="pdbe-citations 1nmo" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Camerini-Otero | <references/> | ||
[[Category: Gilliland | __TOC__ | ||
[[Category: Khil | </StructureSection> | ||
[[Category: Ladner | [[Category: Escherichia coli]] | ||
[[Category: Obmolova | [[Category: Escherichia coli O157:H7]] | ||
[[Category: Large Structures]] | |||
[[Category: Teplyakov | [[Category: Camerini-Otero RD]] | ||
[[Category: Gilliland GL]] | |||
[[Category: Khil PP]] | |||
[[Category: Ladner JE]] | |||
[[Category: Obmolova G]] | |||
[[Category: Teplyakov A]] | |||
Latest revision as of 07:45, 17 October 2024
Structural genomics, protein ybgI, unknown functionStructural genomics, protein ybgI, unknown function
Structural highlights
FunctionGCH1L_ECOLI Provides significant protection from radiation damage and may be involved in the degradation of radiation-damaged nucleotides.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: The protein encoded by the gene ybgI was chosen as a target for a structural genomics project emphasizing the relation of protein structure to function. RESULTS: The structure of the ybgI protein is a toroid composed of six polypeptide chains forming a trimer of dimers. Each polypeptide chain binds two metal ions on the inside of the toroid. CONCLUSION: The toroidal structure is comparable to that of some proteins that are involved in DNA metabolism. The di-nuclear metal site could imply that the specific function of this protein is as a hydrolase-oxidase enzyme. Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site.,Ladner JE, Obmolova G, Teplyakov A, Howard AJ, Khil PP, Camerini-Otero RD, Gilliland GL BMC Struct Biol. 2003 Sep 30;3:7. PMID:14519207[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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