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| | <StructureSection load='4q00' size='340' side='right'caption='[[4q00]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4q00' size='340' side='right'caption='[[4q00]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4q00]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q00 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4q00]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q00 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hyr|3hyr]]</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=4q00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q00 OCA], [https://pdbe.org/4q00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q00 RCSB], [https://www.ebi.ac.uk/pdbsum/4q00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q00 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">feoB, b3409, JW3372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4q00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q00 OCA], [http://pdbe.org/4q00 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q00 RCSB], [http://www.ebi.ac.uk/pdbsum/4q00 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q00 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FEOB_ECOLI FEOB_ECOLI]] GTP-driven Fe(2+) uptake system.<ref>PMID:8407793</ref> <ref>PMID:12446835</ref> | + | [https://www.uniprot.org/uniprot/FEOB_ECOLI FEOB_ECOLI] GTP-driven Fe(2+) uptake system.<ref>PMID:8407793</ref> <ref>PMID:12446835</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Deshpande, C N]] | + | [[Category: Deshpande CN]] |
| - | [[Category: Guilfoyle, A P]] | + | [[Category: Guilfoyle AP]] |
| - | [[Category: Jormakka, M]] | + | [[Category: Jormakka M]] |
| - | [[Category: G protein]]
| + | |
| - | [[Category: Gtp binding]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Iron transport]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
FEOB_ECOLI GTP-driven Fe(2+) uptake system.[1] [2]
Publication Abstract from PubMed
GDP release from GTPases is usually extremely slow and is in general assisted by external factors, such as association with guanine exchange factors or membrane-embedded GPCRs (G protein-coupled receptors), which accelerate the release of GDP by several orders of magnitude. Intrinsic factors can also play a significant role; a single amino acid substitution in one of the guanine nucleotide recognition motifs, G5, results in a drastically altered GDP release rate, indicating that the sequence composition of this motif plays an important role in spontaneous GDP release. In the present study, we used the GTPase domain from EcNFeoB (Escherichia coli FeoB) as a model and applied biochemical and structural approaches to evaluate the role of all the individual residues in the G5 loop. Our study confirms that several of the residues in the G5 motif have an important role in the intrinsic affinity and release of GDP. In particular, a T151A mutant (third residue of the G5 loop) leads to a reduced nucleotide affinity and provokes a drastically accelerated dissociation of GDP.
Exploring the correlation between the sequence composition of the nucleotide binding G5 loop of the FeoB GTPase domain (NFeoB) and intrinsic rate of GDP release.,Guilfoyle AP, Deshpande CN, Schenk G, Maher MJ, Jormakka M Biosci Rep. 2014 Dec 12;34(6):e00158. doi: 10.1042/BSR20140152. PMID:25374115[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kammler M, Schon C, Hantke K. Characterization of the ferrous iron uptake system of Escherichia coli. J Bacteriol. 1993 Oct;175(19):6212-9. PMID:8407793
- ↑ Marlovits TC, Haase W, Herrmann C, Aller SG, Unger VM. The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16243-8. Epub 2002 Nov 22. PMID:12446835 doi:10.1073/pnas.242338299
- ↑ Guilfoyle AP, Deshpande CN, Schenk G, Maher MJ, Jormakka M. Exploring the correlation between the sequence composition of the nucleotide binding G5 loop of the FeoB GTPase domain (NFeoB) and intrinsic rate of GDP release. Biosci Rep. 2014 Dec 12;34(6):e00158. doi: 10.1042/BSR20140152. PMID:25374115 doi:http://dx.doi.org/10.1042/BSR20140152
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