2d3w
From Proteopedia
(Difference between revisions)
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<StructureSection load='2d3w' size='340' side='right'caption='[[2d3w]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2d3w' size='340' side='right'caption='[[2d3w]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2d3w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2d3w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D3W FirstGlance]. <br> |
| - | </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=2d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3w OCA], [https://pdbe.org/2d3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d3w RCSB], [https://www.ebi.ac.uk/pdbsum/2d3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3w ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=2d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3w OCA], [https://pdbe.org/2d3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d3w RCSB], [https://www.ebi.ac.uk/pdbsum/2d3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SUFC_ECOLI SUFC_ECOLI] Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12554644</ref> <ref>PMID:12941942</ref> | |
== 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=2d3w 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=2d3w ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | SufC is an ATPase component of the SUF machinery, which is involved in the biosynthesis of Fe-S clusters. To gain insight into the function of this protein, we have determined the crystal structure of Escherichia coli SufC at 2.5A resolution. Despite the similarity of the overall structure with ABC-ATPases (nucleotide-binding domains of ABC transporters), some key differences were observed. Glu171, an invariant residue involved in ATP hydrolysis, is rotated away from the nucleotide-binding pocket to form a SufC-specific salt bridge with Lys152. Due to this salt bridge, D-loop that follows Glu171 is flipped out to the molecular surface, which may sterically inhibit the formation of an active dimer. Thus, the salt bridge may play a critical role in regulating ATPase activity and preventing wasteful ATP hydrolysis. Furthermore, SufC has a unique Q-loop structure on its surface, which may form a binding site for its partner proteins, SufB and/or SufD. | ||
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| - | Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery.,Kitaoka S, Wada K, Hasegawa Y, Minami Y, Fukuyama K, Takahashi Y FEBS Lett. 2006 Jan 9;580(1):137-43. Epub 2005 Dec 6. PMID:16364320<ref>PMID:16364320</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2d3w" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fukuyama | + | [[Category: Fukuyama K]] |
| - | [[Category: Hasegawa | + | [[Category: Hasegawa Y]] |
| - | [[Category: Kitaoka | + | [[Category: Kitaoka S]] |
| - | [[Category: Minami | + | [[Category: Minami Y]] |
| - | [[Category: Takahashi | + | [[Category: Takahashi Y]] |
| - | [[Category: Wada | + | [[Category: Wada K]] |
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Current revision
Crystal Structure of Escherichia coli SufC, an ATPase compenent of the SUF iron-sulfur cluster assembly machinery
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