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==THE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR== | |||
<StructureSection load='1hrr' size='340' side='right'caption='[[1hrr]]' scene=''> | |||
| | == Structural highlights == | ||
| | <table><tr><td colspan='2'>[[1hrr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRR FirstGlance]. <br> | ||
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=1hrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrr OCA], [https://pdbe.org/1hrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrr RCSB], [https://www.ebi.ac.uk/pdbsum/1hrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HIP_ALLVD HIP_ALLVD] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. | |||
== 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/hr/1hrr_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1hrr ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639] has been extended up to 85% of the total protein protons. Ninety percent of the nitrogens have been assigned. Then the solution structure has been obtained using as many as 1147 meaningful NOE connectivities. The protein is sizably paramagnetic even though the ground state is a singlet. Nevertheless, the final RMSD values are 0.62 and 1.19 A for the backbone and the heavy atoms, respectively. These values compare well with those for diamagnetic proteins of the same size. The solution structure is discussed in the light of the available structural information from X-ray data. | The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639] has been extended up to 85% of the total protein protons. Ninety percent of the nitrogens have been assigned. Then the solution structure has been obtained using as many as 1147 meaningful NOE connectivities. The protein is sizably paramagnetic even though the ground state is a singlet. Nevertheless, the final RMSD values are 0.62 and 1.19 A for the backbone and the heavy atoms, respectively. These values compare well with those for diamagnetic proteins of the same size. The solution structure is discussed in the light of the available structural information from X-ray data. | ||
The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.,Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P Biochemistry. 1995 Jan 10;34(1):206-19. PMID:7819198<ref>PMID:7819198</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hrr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Allochromatium vinosum]] | [[Category: Allochromatium vinosum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Banci | [[Category: Banci L]] | ||
[[Category: Bertini | [[Category: Bertini I]] | ||
[[Category: Dikiy | [[Category: Dikiy A]] | ||
[[Category: Kastrau | [[Category: Kastrau DHW]] | ||
[[Category: Luchinat | [[Category: Luchinat C]] | ||
[[Category: Sompornpisut | [[Category: Sompornpisut P]] | ||
Latest revision as of 11:32, 22 May 2024
THE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMRTHE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR
Structural highlights
FunctionHIP_ALLVD Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. 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 PubMedThe 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639] has been extended up to 85% of the total protein protons. Ninety percent of the nitrogens have been assigned. Then the solution structure has been obtained using as many as 1147 meaningful NOE connectivities. The protein is sizably paramagnetic even though the ground state is a singlet. Nevertheless, the final RMSD values are 0.62 and 1.19 A for the backbone and the heavy atoms, respectively. These values compare well with those for diamagnetic proteins of the same size. The solution structure is discussed in the light of the available structural information from X-ray data. The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.,Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P Biochemistry. 1995 Jan 10;34(1):206-19. PMID:7819198[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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