3qzo: Difference between revisions

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<StructureSection load='3qzo' size='340' side='right'caption='[[3qzo]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3qzo' size='340' side='right'caption='[[3qzo]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qzo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staan Staan]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QZO FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qzo]] is a 4 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=3QZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QZO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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]] 1.952&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">frpA, isdA, SA0977, stbA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158879 STAAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=3qzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qzo OCA], [https://pdbe.org/3qzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qzo RCSB], [https://www.ebi.ac.uk/pdbsum/3qzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qzo 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=3qzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qzo OCA], [https://pdbe.org/3qzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qzo RCSB], [https://www.ebi.ac.uk/pdbsum/3qzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qzo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ISDA_STAAN ISDA_STAAN]] Transfers its hemin to hemin-free IsdC (apo-IsdC) directly probably through the activated holo-IsdA-apo-IsdC complex and driven by the higher affinity of apo-IsdC for the cofactor. The reaction is reversible. Binds transferrin, lactoferrin, heme, hemoglobin, hemin, fetuin, asialofetuin and protein A. Also binds fibronectin and chains B-beta and gamma of fibrinogen. Could play a role in the removal of heme from hemoglobin. The IsdA-mediated iron-acquisition system from transferrin could play only an ancillary role in the iron uptake whereas the siderophore-mediated iron-acquisition system from transferrin seems to play an essential or dominant role. May function as a reservoir for heme. Involved in adherence of S.aureus to human desquamated nasal epithelial cells and is required for nasal colonization. Protects S.aureus against the bactericidal protease activity of apolactoferrin in vitro and confers resistance to bovine lactoferricin. Also IsdA and/or IsdB promote resistance to hydrogen peroxide and killing by neutrophils (By similarity).  
[https://www.uniprot.org/uniprot/ISDA_STAAN ISDA_STAAN] Transfers its hemin to hemin-free IsdC (apo-IsdC) directly probably through the activated holo-IsdA-apo-IsdC complex and driven by the higher affinity of apo-IsdC for the cofactor. The reaction is reversible. Binds transferrin, lactoferrin, heme, hemoglobin, hemin, fetuin, asialofetuin and protein A. Also binds fibronectin and chains B-beta and gamma of fibrinogen. Could play a role in the removal of heme from hemoglobin. The IsdA-mediated iron-acquisition system from transferrin could play only an ancillary role in the iron uptake whereas the siderophore-mediated iron-acquisition system from transferrin seems to play an essential or dominant role. May function as a reservoir for heme. Involved in adherence of S.aureus to human desquamated nasal epithelial cells and is required for nasal colonization. Protects S.aureus against the bactericidal protease activity of apolactoferrin in vitro and confers resistance to bovine lactoferricin. Also IsdA and/or IsdB promote resistance to hydrogen peroxide and killing by neutrophils (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Staan]]
[[Category: Staphylococcus aureus subsp. aureus N315]]
[[Category: Grigg, J C]]
[[Category: Grigg JC]]
[[Category: Mao, C X]]
[[Category: Mao CX]]
[[Category: Murphy, M E.P]]
[[Category: Murphy MEP]]
[[Category: Cell wall]]
[[Category: Ferrous]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Metal binding protein]]
[[Category: Receptor]]
[[Category: Transport]]
[[Category: Uptake]]
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