3li2

<StructureSection load='3li2' size='340' side='right' caption='[[3li2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[3li2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staae Staae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LI2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SF8:(2R)-2-(2-{[(1R)-1-CARBOXY-4-{[(3S)-3,4-DICARBOXY-3-HYDROXYBUTANOYL]AMINO}BUTYL]AMINO}-2-OXOETHYL)-2-HYDROXYBUTANEDIOIC+ACID'>SF8</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">htsA, NWMN_2078 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=426430 STAAE])</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=3li2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3li2 OCA], [http://pdbe.org/3li2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3li2 RCSB], [http://www.ebi.ac.uk/pdbsum/3li2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3li2 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Staphylococcus aureus uses several efficient iron acquisition strategies to overcome iron limitation. Recently, the genetic locus encoding biosynthetic enzymes for the iron chelating molecule, staphyloferrin A (SA), was determined. S. aureus synthesizes and secretes SA into its environment to scavenge iron. The membrane-anchored ATP binding cassette-binding protein, HtsA, receives the ferric-chelate for import into the cell. Recently, we determined the apoHtsA crystal structure, the first siderophore receptor from gram-positive bacteria to be structurally characterized. Herein we present the x-ray crystal structure of the HtsA-ferric-SA complex. HtsA adopts a class III binding protein fold composed of separate N- and C-terminal domains bridged by a single alpha-helix. Recombinant HtsA can efficiently sequester ferric-SA from S. aureus culture supernatants where it is bound within the pocket formed between distinct N- and C-terminal domains. A basic patch composed mainly of six Arg residues contact the negatively charged siderophore, securing it within the pocket. The x-ray crystal structures from two different ligand-bound crystal forms were determined. The structures represent the first structural characterization of an endogenous alpha-hydroxycarboxylate-type siderophore-receptor complex. One structure is in an open form similar to apoHtsA, whereas the other is in a more closed conformation. The conformational change is highlighted by isolated movement of three loops within the C-terminal domain, a domain movement unique to known class III binding protein structures.

The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket.,Grigg JC, Cooper JD, Cheung J, Heinrichs DE, Murphy ME J Biol Chem. 2010 Apr 9;285(15):11162-71. Epub 2010 Feb 10. PMID:20147287<ref>PMID:20147287</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3li2" style="background-color:#fffaf0;"></div>

*[[ABC transporter|ABC transporter]]

[[Category: Staae]]

[[Category: Grigg, J C]]

[[Category: Murphy, M E.P]]

[[Category: Binding protein]]

[[Category: Iron]]

[[Category: Transport protein]]