1d9v: Difference between revisions

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<StructureSection load='1d9v' size='340' side='right'caption='[[1d9v]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='1d9v' size='340' side='right'caption='[[1d9v]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1d9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D9V FirstGlance]. <br>
<table><tr><td colspan='2'>[[1d9v]] 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=1D9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D9V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.75&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mrp|1mrp]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HITA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</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=1d9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9v OCA], [https://pdbe.org/1d9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d9v RCSB], [https://www.ebi.ac.uk/pdbsum/1d9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9v 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=1d9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9v OCA], [https://pdbe.org/1d9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d9v RCSB], [https://www.ebi.ac.uk/pdbsum/1d9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1d9v ConSurf].
</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=1d9v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the iron-free (apo) form of the Haemophilus influenzae Fe(3+)-binding protein (hFbp) has been determined to 1.75 A resolution. Information from this structure complements that derived from the holo structure with respect to the delineation of the process of iron binding and release. A 21 degrees rotation separates the two structural domains when the apo form is compared with the holo conformer, indicating that upon release of iron, the protein undergoes a change in conformation by bending about the central beta-sheet hinge. A surprising finding in the apo-hFbp structure was that the ternary binding site anion, observed in the crystals as phosphate, remained bound. In solution, apo-hFbp bound phosphate with an affinity K(d) of 2.3 x 10(-3) M. The presence of this ternary binding site anion appears to arrange the C-terminal iron-binding residues conducive to complementary binding to Fe(3+), while residues in the N-terminal binding domain must undergo induced fit to accommodate the Fe(3+) ligand. These observations suggest a binding process, the first step of which is the binding of a synergistic anion such as phosphate to the C-terminal domain. Next, iron binds to the preordered half-site on the C-terminal domain. Finally, the presence of iron organizes the N-terminal half-site and closes the interdomain hinge. The use of the synergistic anion and this iron binding process results in an extremely high affinity of the Fe(3+)-binding proteins for Fe(3+) (nFbp K'(eff) = 2.4 x 10(18) M(-1)). This high-affinity ligand binding process is unique among the family of bacterial periplasmic binding proteins and has interesting implications in the mechanism of iron removal from the Fe(3+)-binding proteins during FbpABC-mediated iron transport across the cytoplasmic membrane.
Crystallographic and biochemical analyses of the metal-free Haemophilus influenzae Fe3+-binding protein.,Bruns CM, Anderson DS, Vaughan KG, Williams PA, Nowalk AJ, McRee DE, Mietzner TA Biochemistry. 2001 Dec 25;40(51):15631-7. PMID:11747438<ref>PMID:11747438</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1d9v" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ferric-binding protein|Ferric-binding protein]]
*[[Ferric-binding protein|Ferric-binding protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium influenzae lehmann and neumann 1896]]
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bruns, C M]]
[[Category: Bruns CM]]
[[Category: McRee, D E]]
[[Category: McRee DE]]
[[Category: Williams, P A]]
[[Category: Williams PA]]
[[Category: Abc cassette receptor protein]]
[[Category: Apo form]]
[[Category: Binding protein]]
[[Category: Ferric]]
[[Category: Iron]]
[[Category: Metal binding protein]]
[[Category: Periplasmic protein]]

Latest revision as of 09:51, 7 February 2024

HAEMOPHILUS INFLUENZAE FERRIC-BINDING PROTEIN APO FORMHAEMOPHILUS INFLUENZAE FERRIC-BINDING PROTEIN APO FORM

Structural highlights

1d9v is a 1 chain structure with sequence from Haemophilus influenzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1d9v, resolution 1.75Å

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