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| | ==Solution structure of Staphylococcus aureus IsdH linker domain== | | ==Solution structure of Staphylococcus aureus IsdH linker domain== |
| - | <StructureSection load='2lhr' size='340' side='right' caption='[[2lhr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lhr' size='340' side='right'caption='[[2lhr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lhr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staaw Staaw]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LHR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lhr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LHR FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">isdH, harA, sasI, MW1674 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=196620 STAAW])</td></tr> | + | </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='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=2lhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhr OCA], [http://pdbe.org/2lhr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lhr RCSB], [http://www.ebi.ac.uk/pdbsum/2lhr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lhr ProSAT]</span></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=2lhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhr OCA], [https://pdbe.org/2lhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lhr RCSB], [https://www.ebi.ac.uk/pdbsum/2lhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lhr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ISDH_STAAW ISDH_STAAW]] Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (By similarity). | + | [https://www.uniprot.org/uniprot/ISDH_STAAW ISDH_STAAW] Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Staaw]] | + | [[Category: Large Structures]] |
| - | [[Category: Clubb, R T]] | + | [[Category: Staphylococcus aureus subsp. aureus MW2]] |
| - | [[Category: Malmirchegini, G R]] | + | [[Category: Clubb RT]] |
| - | [[Category: Robson, S A]] | + | [[Category: Malmirchegini GR]] |
| - | [[Category: Spirig, T]] | + | [[Category: Robson SA]] |
| - | [[Category: Heme acquisition]] | + | [[Category: Spirig T]] |
| - | [[Category: Hemoglobin receptor]]
| + | |
| - | [[Category: Iron uptake]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Neat domain]]
| + | |
| Structural highlights
Function
ISDH_STAAW Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (By similarity).
Publication Abstract from PubMed
Staphylococcus aureus is a leading cause of life-threatening infections in the United States. It requires iron to grow, which must be actively procured from its host to successfully mount an infection. Heme-iron within hemoglobin (Hb) is the most abundant source of iron in the human body and is captured by S. aureus using two closely related receptors, IsdH and IsdB. Here we demonstrate that each receptor captures heme using two conserved near iron transporter (NEAT) domains that function synergistically. NMR studies of the 39-kDa conserved unit from IsdH (IsdH(N2N3), Ala(326)-Asp(660)) reveals that it adopts an elongated dumbbell-shaped structure in which its NEAT domains are properly positioned by a helical linker domain, whose three-dimensional structure is determined here in detail. Electrospray ionization mass spectrometry and heme transfer measurements indicate that IsdH(N2N3) extracts heme from Hb via an ordered process in which the receptor promotes heme release by inducing steric strain that dissociates the Hb tetramer. Other clinically significant Gram-positive pathogens capture Hb using receptors that contain multiple NEAT domains, suggesting that they use a conserved mechanism.
Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme.,Spirig T, Malmirchegini GR, Zhang J, Robson SA, Sjodt M, Liu M, Krishna Kumar K, Dickson CF, Gell DA, Lei B, Loo JA, Clubb RT J Biol Chem. 2013 Jan 11;288(2):1065-78. doi: 10.1074/jbc.M112.419119. Epub 2012 , Nov 6. PMID:23132864[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Spirig T, Malmirchegini GR, Zhang J, Robson SA, Sjodt M, Liu M, Krishna Kumar K, Dickson CF, Gell DA, Lei B, Loo JA, Clubb RT. Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme. J Biol Chem. 2013 Jan 11;288(2):1065-78. doi: 10.1074/jbc.M112.419119. Epub 2012 , Nov 6. PMID:23132864 doi:http://dx.doi.org/10.1074/jbc.M112.419119
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