2itf: Difference between revisions

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 <StructureSection load='2itf' size='340' side='right'caption='[[2itf]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2itf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ITF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ITF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2itf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ITF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ITF FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">isdA, frpA, stbA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=2itf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2itf OCA], [https://pdbe.org/2itf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2itf RCSB], [https://www.ebi.ac.uk/pdbsum/2itf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2itf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ISDA_STAAW ISDA_STAAW]] 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 (By similarity). Also IsdA and/or IsdB promote resistance to hydrogen peroxide and killing by neutrophils.<ref>PMID:18097052</ref> <ref>PMID:18184657</ref>
+[https://www.uniprot.org/uniprot/ISDA_STAA8 ISDA_STAA8] Cell wall-anchored surface receptor that participates in the extraction of heme from oxidized methemoglobin/metHb to enable growth on hemoglobin as a sole iron source (By similarity). Receives heme from IsdB and transfers it to IsdC (By similarity). Also plays a role in the inhibition of host immune response. Protects S.aureus against the bactericidal protease activity of apolactoferrin. Decreases bacterial cellular hydrophobicity, which renders S.aureus resistant to bactericidal human skin fatty acids as well as to beta-defensins and cathelicidin. Also binds fibronectin and chains B-beta and gamma of fibrinogen, promoting clumping of S.aureus with fibrinogen. Involved in adherence of S.aureus to human desquamated nasal epithelial cells and is required for nasal colonization (By similarity).[UniProtKB:A6QG31][UniProtKB:Q7A152]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/it/2itf_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 35: / Line 34: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Grigg, J C]]
+[[Category: Staphylococcus aureus]]
-[[Category: Heinrichs, D E]]
+[[Category: Grigg JC]]
-[[Category: Murphy, M E]]
+[[Category: Heinrichs DE]]
-[[Category: Vermeiren, C L]]
+[[Category: Murphy ME]]
-[[Category: Heme]]
+[[Category: Vermeiren CL]]
-[[Category: Iron]]
-[[Category: Metal binding protein]]
-[[Category: Neat domain]]