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| | ==Crystal Structure of S. aureus IsdE complexed with heme== | | ==Crystal Structure of S. aureus IsdE complexed with heme== |
| - | <StructureSection load='2q8q' size='340' side='right' caption='[[2q8q]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='2q8q' size='340' side='right'caption='[[2q8q]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2q8q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staan Staan]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q8Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q8Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2q8q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_N315 Staphylococcus aureus subsp. aureus N315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q8Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q8p|2q8p]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">isdA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158879 STAAN])</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=2q8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q8q OCA], [https://pdbe.org/2q8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q8q RCSB], [https://www.ebi.ac.uk/pdbsum/2q8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q8q ProSAT]</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=2q8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q8q OCA], [http://pdbe.org/2q8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q8q RCSB], [http://www.ebi.ac.uk/pdbsum/2q8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q8q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ISDE_STAAN ISDE_STAAN]] Involved in heme (porphyrin) scavenging. Binds Fe(2+) and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a high-affinity heme binding protein and probably has a role in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF (By similarity). | + | [https://www.uniprot.org/uniprot/ISDE_STAAN ISDE_STAAN] Involved in heme (porphyrin) scavenging. Binds Fe(2+) and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a high-affinity heme binding protein and probably has a role in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q8/2q8q_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q8/2q8q_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Staan]] | + | [[Category: Large Structures]] |
| - | [[Category: Grigg, J C]] | + | [[Category: Staphylococcus aureus subsp. aureus N315]] |
| - | [[Category: Murphy, M E]] | + | [[Category: Grigg JC]] |
| - | [[Category: Helical backbone metal receptor superfamily]] | + | [[Category: Murphy ME]] |
| - | [[Category: Metal transport]]
| + | |
| Structural highlights
Function
ISDE_STAAN Involved in heme (porphyrin) scavenging. Binds Fe(2+) and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a high-affinity heme binding protein and probably has a role in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF (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
Staphylococcus aureus is a Gram-positive bacterial pathogen and a leading cause of hospital acquired infections. Because the free iron concentration in the human body is too low to support growth, S. aureus must acquire iron from host sources. Heme iron is the most prevalent iron reservoir in the human body and a predominant source of iron for S. aureus. The iron-regulated surface determinant (Isd) system removes heme from host heme proteins and transfers it to IsdE, the cognate substrate-binding lipoprotein of an ATP-binding cassette transporter, for import and subsequent degradation. Herein, we report the crystal structure of the soluble portion of the IsdE lipoprotein in complex with heme. The structure reveals a bi-lobed topology formed by an N- and C-terminal domain bridged by a single alpha-helix. The structure places IsdE as a member of the helical backbone metal receptor superfamily. A six-coordinate heme molecule is bound in the groove established at the domain interface, and the heme iron is coordinated in a novel fashion for heme transporters by Met(78) and His(229). Both heme propionate groups are secured by H-bonds to IsdE main chain and side chain groups. Of these residues, His(229) is essential for IsdE-mediated heme uptake by S. aureus when growth on heme as a sole iron source is measured. Multiple sequence alignments of homologues from several other Gram-positive bacteria, including the human pathogens pyogenes, Bacillus anthracis, and Listeria monocytogenes, suggest that these other systems function equivalently to S. aureus IsdE with respect to heme binding and transport.
Heme coordination by Staphylococcus aureus IsdE.,Grigg JC, Vermeiren CL, Heinrichs DE, Murphy ME J Biol Chem. 2007 Sep 28;282(39):28815-22. Epub 2007 Jul 31. PMID:17666394[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grigg JC, Vermeiren CL, Heinrichs DE, Murphy ME. Heme coordination by Staphylococcus aureus IsdE. J Biol Chem. 2007 Sep 28;282(39):28815-22. Epub 2007 Jul 31. PMID:17666394 doi:10.1074/jbc.M704602200
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