3fvq

<StructureSection load='3fvq' size='340' side='right' caption='[[3fvq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[3fvq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neig1 Neig1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FVQ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fbpC, NGO0215 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242231 NEIG1])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fe(3+)-transporting_ATPase Fe(3+)-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.30 3.6.3.30] </span></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=3fvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fvq OCA], [http://pdbe.org/3fvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fvq RCSB], [http://www.ebi.ac.uk/pdbsum/3fvq PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/FBPC_NEIG1 FBPC_NEIG1]] Part of the ABC transporter complex FbpABC involved in Fe(3+) ions import. Responsible for energy coupling to the transport system (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/3fvq_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The mechanism by which nucleotide-binding domains (NBDs) of ABC transporters power the transport of substrates across cell membranes is currently unclear. Here we report the crystal structure of an NBD, FbpC, from the Neisseria gonorrhoeae ferric iron uptake transporter with an unusual and substantial domain swap in the C-terminal regulatory domain. This entanglement suggests that FbpC is unable to open to the same extent as the homologous protein MalK. Using molecular dynamics we demonstrate that this is not the case: both NBDs open rapidly once ATP is removed. We conclude from this result that the closed structures of FbpC and MalK have higher free energies than their respective open states. This result has important implications for our understanding of the mechanism of power generation in ABC transporters, because the unwinding of this free energy ensures that the opening of these two NBDs is also powered.

Insights into how nucleotide-binding domains power ABC transport.,Newstead S, Fowler PW, Bilton P, Carpenter EP, Sadler PJ, Campopiano DJ, Sansom MS, Iwata S Structure. 2009 Sep 9;17(9):1213-22. PMID:19748342<ref>PMID:19748342</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 3fvq" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Neig1]]

[[Category: Bilton, P]]

[[Category: Campopiano, D]]

[[Category: Carpenter, E P]]

[[Category: Iwata, S]]

[[Category: Newstead, S]]

[[Category: Transport]]