1mrp

<table><tr><td colspan='2'>[[1mrp]] is a 1 chain structure with sequence from [http://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=1MRP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MRP FirstGlance]. <br>

</td></tr><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>, <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 ([http://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'>[http://proteopedia.org/fgij/fg.htm?mol=1mrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mrp OCA], [http://pdbe.org/1mrp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mrp RCSB], [http://www.ebi.ac.uk/pdbsum/1mrp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mrp ProSAT]</span></td></tr>

[[http://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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== Publication Abstract from PubMed ==

The first crystal structure of the iron-transporter ferric ion-binding protein from Haemophilus influenzae (hFBP), at 1.6 A resolution, reveals the structural basis for iron uptake and transport required by several important bacterial pathogens. Paradoxically, although hFBP belongs to a protein superfamily which includes human transferrin, iron binding in hFBP and transferrin appears to have developed independently by convergent evolution. Structural comparison of hFBP with other prokaryotic periplasmic transport proteins and the eukaryotic transferrins suggests that these proteins are related by divergent evolution from an anion-binding common ancestor, not from an iron-binding ancestor. The iron binding site of hFBP incorporates a water and an exogenous phosphate ion as iron ligands and exhibits nearly ideal octahedral metal coordination. FBP is highly conserved, required for virulence, and is a nodal point for free iron uptake in several Gram-negative pathogenic bacteria, thus providing a potential target for broad-spectrum antibacterial drug design against human pathogens such as H. influenzae, Neisseria gonorrhoeae, and Neisseria meningitidis.

Structure of Haemophilus influenzae Fe(+3)-binding protein reveals convergent evolution within a superfamily.,Bruns CM, Nowalk AJ, Arvai AS, McTigue MA, Vaughan KG, Mietzner TA, McRee DE Nat Struct Biol. 1997 Nov;4(11):919-24. PMID:9360608<ref>PMID:9360608</ref>

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

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== References ==

<references/>

[[Category: Bacterium influenzae lehmann and neumann 1896]]

[[Category: Arvai, A S]]

[[Category: Bruns, C M]]

[[Category: Mcree, D E]]

[[Category: Mctigue, M A]]

[[Category: Mietzner, T A]]

[[Category: Nowalk, A J]]

[[Category: Vaughan, K G]]

[[Category: Transferrin superfamily]]