2o69

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[[Image:2o69.jpg|left|200px]]
 
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==Crystal Structure of Haemophilus influenzae N193L mutant FbpA==
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The line below this paragraph, containing "STRUCTURE_2o69", creates the "Structure Box" on the page.
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<StructureSection load='2o69' size='340' side='right'caption='[[2o69]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2o69]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O69 FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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{{STRUCTURE_2o69| PDB=2o69 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o69 OCA], [https://pdbe.org/2o69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o69 RCSB], [https://www.ebi.ac.uk/pdbsum/2o69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o69 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FBPA_HAEIN FBPA_HAEIN] Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein specifically binds Fe(3+) and is involved in its transmembrane transport (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/2o69_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o69 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The acquisition of iron from transferrin by Gram-negative bacterial pathogens is dependent on a periplasmic ferric-ion-binding protein, FbpA. FbpA shuttles iron from the outer membrane to an inner membrane transport complex. A bound phosphate anion completes the iron co-ordination shell of FbpA and kinetic studies demonstrate that the anion plays a critical role in iron binding and release in vitro. The present study was initiated to directly address the hypothesis that the synergistic anion is required for transport of iron in intact cells. A series of site-directed mutants in the anion-binding amino acids of the Haemophilus influenzae FbpA (Gln-58, Asn-175 and Asn-193) were prepared to provide proteins defective in binding of the phosphate anion. Crystal structures of various mutants have revealed that alteration of the C-terminal domain ligands (Asn-175 or Asn-193) but not the N-terminal domain ligand (Gln-58) abrogated binding of the phosphate anion. The mutant proteins were introduced into H. influenzae to evaluate their ability to mediate iron transport. All of the single site-directed mutants (Q58L, N175L and N193L) were capable of mediating iron acquisition from transferrin and from limiting concentrations of ferric citrate. The results suggest that the transport of iron by FbpA is not dependent on binding of phosphate in the synergistic anion-binding site.
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'''Crystal Structure of Haemophilus influenzae N193L mutant FbpA'''
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The role of the synergistic phosphate anion in iron transport by the periplasmic iron-binding protein from Haemophilus influenzae.,Khan AG, Shouldice SR, Tari LW, Schryvers AB Biochem J. 2007 Apr 1;403(1):43-8. PMID:17147516<ref>PMID:17147516</ref>
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==Overview==
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The acquisition of iron from transferrin by Gram-negative bacterial pathogens is dependent on a periplasmic ferric-ion-binding protein, FbpA. FbpA shuttles iron from the outer membrane to an inner membrane transport complex. A bound phosphate anion completes the iron co-ordination shell of FbpA and kinetic studies demonstrate that the anion plays a critical role in iron binding and release in vitro. The present study was initiated to directly address the hypothesis that the synergistic anion is required for transport of iron in intact cells. A series of site-directed mutants in the anion-binding amino acids of the Haemophilus influenzae FbpA (Gln-58, Asn-175 and Asn-193) were prepared to provide proteins defective in binding of the phosphate anion. Crystal structures of various mutants have revealed that alteration of the C-terminal domain ligands (Asn-175 or Asn-193) but not the N-terminal domain ligand (Gln-58) abrogated binding of the phosphate anion. The mutant proteins were introduced into H. influenzae to evaluate their ability to mediate iron transport. All of the single site-directed mutants (Q58L, N175L and N193L) were capable of mediating iron acquisition from transferrin and from limiting concentrations of ferric citrate. The results suggest that the transport of iron by FbpA is not dependent on binding of phosphate in the synergistic anion-binding site.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2O69 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O69 OCA].
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</div>
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<div class="pdbe-citations 2o69" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The role of the synergistic phosphate anion in iron transport by the periplasmic iron-binding protein from Haemophilus influenzae., Khan AG, Shouldice SR, Tari LW, Schryvers AB, Biochem J. 2007 Apr 1;403(1):43-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17147516 17147516]
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*[[Ferric-binding protein|Ferric-binding protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Shouldice, S R.]]
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[[Category: Shouldice SR]]
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[[Category: Tari, L W.]]
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[[Category: Tari LW]]
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[[Category: Iron binding]]
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[[Category: Mixed beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:22:51 2008''
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Current revision

Crystal Structure of Haemophilus influenzae N193L mutant FbpA

PDB ID 2o69

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