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1h98

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[[Image:1h98.gif|left|200px]]
 
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{{Structure
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==New Insights into Thermostability of Bacterial Ferredoxins: High Resolution Crystal Structure of the Seven-Iron Ferredoxin from Thermus thermophilus==
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|PDB= 1h98 |SIZE=350|CAPTION= <scene name='initialview01'>1h98</scene>, resolution 1.64&Aring;
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<StructureSection load='1h98' size='340' side='right'caption='[[1h98]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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|SITE= <scene name='pdbsite=FS4:CYS+Residues+8,+16+And+49+Coordinate+The+Fs3'>FS4</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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<table><tr><td colspan='2'>[[1h98]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H98 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h98 OCA], [https://pdbe.org/1h98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h98 RCSB], [https://www.ebi.ac.uk/pdbsum/1h98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h98 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h98 OCA], [http://www.ebi.ac.uk/pdbsum/1h98 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h98 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/FER_THET8 FER_THET8] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/1h98_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1h98 ConSurf].
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<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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The crystal structure of the seven-iron ferredoxin from Thermus thermophilus (FdTt) has been determined at 1.64 A resolution, allowing us to unveil the common mechanisms of thermostabilization within "bacterial-type" ferredoxins. FdTt and other homologous thermophilic seven-iron ferredoxins are smaller than their mesophilic counterparts. Thermostabilizing features are optimized in a minimal structural and functional unit, with an extensive cross-linking of secondary structure elements mediated by improved polar and hydrophobic interactions. Most of the potentially stabilizing features are focused on the vicinity of the functional [3Fe-4S] cluster. The structural [4Fe-4S] cluster is shielded in thermophilic FdTt by an increased number of polar interactions involving the two N-terminal residues. Comparisons with the hyperthermostable ferredoxin from Thermotoga maritima reveal that (1) a reduction in the number of non-glycine residues in strained conformations, (2) improved polar interactions within the common iron-sulfur cluster binding (betaalphabeta)2 motif, and (3) an optimized charge distribution at the protein surface, constitute a common strategy for increasing the thermal stability of these ferredoxins.
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'''NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS'''
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New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus.,Macedo-Ribeiro S, Martins BM, Pereira PJ, Buse G, Huber R, Soulimane T J Biol Inorg Chem. 2001 Sep;6(7):663-74. PMID:11681700<ref>PMID:11681700</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 1h98" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The crystal structure of the seven-iron ferredoxin from Thermus thermophilus (FdTt) has been determined at 1.64 A resolution, allowing us to unveil the common mechanisms of thermostabilization within "bacterial-type" ferredoxins. FdTt and other homologous thermophilic seven-iron ferredoxins are smaller than their mesophilic counterparts. Thermostabilizing features are optimized in a minimal structural and functional unit, with an extensive cross-linking of secondary structure elements mediated by improved polar and hydrophobic interactions. Most of the potentially stabilizing features are focused on the vicinity of the functional [3Fe-4S] cluster. The structural [4Fe-4S] cluster is shielded in thermophilic FdTt by an increased number of polar interactions involving the two N-terminal residues. Comparisons with the hyperthermostable ferredoxin from Thermotoga maritima reveal that (1) a reduction in the number of non-glycine residues in strained conformations, (2) improved polar interactions within the common iron-sulfur cluster binding (betaalphabeta)2 motif, and (3) an optimized charge distribution at the protein surface, constitute a common strategy for increasing the thermal stability of these ferredoxins.
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1H98 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H98 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus., Macedo-Ribeiro S, Martins BM, Pereira PJ, Buse G, Huber R, Soulimane T, J Biol Inorg Chem. 2001 Sep;6(7):663-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11681700 11681700]
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[[Category: Single protein]]
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[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: Buse, G.]]
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[[Category: Buse G]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Macedo-Ribeiro, S.]]
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[[Category: Macedo-Ribeiro S]]
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[[Category: Martins, B M.]]
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[[Category: Martins BM]]
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[[Category: Pereira, P J.B.]]
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[[Category: Pereira PJB]]
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[[Category: Soulimane, T.]]
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[[Category: Soulimane T]]
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[[Category: azotobacter]]
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[[Category: high resolution]]
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[[Category: hydrogen bond]]
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[[Category: iron-sulfur]]
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[[Category: stability]]
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[[Category: thermophilic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:00:23 2008''
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Current revision

New Insights into Thermostability of Bacterial Ferredoxins: High Resolution Crystal Structure of the Seven-Iron Ferredoxin from Thermus thermophilus

PDB ID 1h98

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