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1q48

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Revision as of 04:03, 10 September 2015

Solution NMR Structure of The Haemophilus Influenzae Iron-Sulfur Cluster Assembly Protein U (IscU) with Zinc Bound at the Active Site. Northeast Structural Genomics Consortium Target IR24. This protein is not apo, it is a model without zinc binding constraints.

Structural highlights

1q48 is a 1 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	HI0377 ("Bacterium influenzae" Lehmann and Neumann 1896)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN

Function

[ISCU_HAEIN] A scaffold on which IscS assembles Fe-S clusters. Subsequently gives the nascent cluster to other proteins. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (By similarity).

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 PubMed

IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur ([Fe-S]) clusters. We report the NMR solution structure of monomeric Haemophilus influenzae IscU with zinc bound at the [Fe-S] cluster assembly site. The compact core of the globular structure has an alpha-beta sandwich architecture with a three-stranded antiparallel beta-sheet and four alpha-helices. A nascent helix is located N-terminal to the core structure. The zinc is ligated by three cysteine residues and one histidine residue that are located in and near conformationally dynamic loops at one end of the IscU structure. Removal of the zinc metal by chelation results in widespread loss of structure in the apo form. The zinc-bound IscU may be a good model for iron-loaded IscU and may demonstrate structural features found in the [Fe-S] cluster bound form. Structural and functional similarities, genomic context in operons containing other homologous genes, and distributions of conserved surface residues support the hypothesis that IscU protein domains are homologous (i.e. derived from a common ancestor) with the SufE/YgdK family of [Fe-S] cluster assembly proteins.

Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.,Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA J Mol Biol. 2004 Nov 19;344(2):567-83. PMID:15522305^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA. Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site. J Mol Biol. 2004 Nov 19;344(2):567-83. PMID:15522305 doi:10.1016/j.jmb.2004.08.038

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q48"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1q48]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q48 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HI0377 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q48 RCSB], [http://www.ebi.ac.uk/pdbsum/1q48 PDBsum], [http://www.topsan.org/Proteins/NESGC/1q48 TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q48 OCA], [http://pdbe.org/1q48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q48 RCSB], [http://www.ebi.ac.uk/pdbsum/1q48 PDBsum], [http://www.topsan.org/Proteins/NESGC/1q48 TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1q48" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1q48

From Proteopedia

Revision as of 04:03, 10 September 2015

Solution NMR Structure of The Haemophilus Influenzae Iron-Sulfur Cluster Assembly Protein U (IscU) with Zinc Bound at the Active Site. Northeast Structural Genomics Consortium Target IR24. This protein is not apo, it is a model without zinc binding constraints.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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