3a1s: Difference between revisions
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==Crystal structue of the cytosolic domain of T. maritima FeoB iron iransporter in GDP form I== | ==Crystal structue of the cytosolic domain of T. maritima FeoB iron iransporter in GDP form I== | ||
<StructureSection load='3a1s' size='340' side='right' caption='[[3a1s]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='3a1s' size='340' side='right' caption='[[3a1s]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ait|3ait]], [[3aiu|3aiu]], [[3aiv|3aiv]], [[3aiw|3aiw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ait|3ait]], [[3aiu|3aiu]], [[3aiv|3aiv]], [[3aiw|3aiw]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM0051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM0051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=3a1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1s OCA], [http://pdbe.org/3a1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a1s RCSB], [http://www.ebi.ac.uk/pdbsum/3a1s PDBsum]</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=3a1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1s OCA], [http://pdbe.org/3a1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a1s RCSB], [http://www.ebi.ac.uk/pdbsum/3a1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a1s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/3a1s_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/3a1s_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 09:50, 18 October 2018
Crystal structue of the cytosolic domain of T. maritima FeoB iron iransporter in GDP form ICrystal structue of the cytosolic domain of T. maritima FeoB iron iransporter in GDP form I
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe FeoB family proteins are widely distributed prokaryotic membrane proteins involved in Fe(2+) uptake. FeoB consists of N-terminal cytosolic and C-terminal transmembrane domains. The N-terminal region of the cytosolic domain is homologous to small GTPase (G) proteins and is considered to regulate Fe(2+) uptake. The spacer region connecting the G and TM domains reportedly functions as a GDP dissociation inhibitor (GDI)-like domain that stabilizes the GDP-binding state. However, the function of the G and GDI-like domains in iron uptake remains unclear. Here, we report the structural and functional analyses of the FeoB cytosolic domain from Thermotoga maritima. The structure-based mutational analysis indicated that the interaction between the G and GDI-like domains is important for both the GDI and Fe(2+) uptake activities. On the basis of these results, we propose a regulatory mechanism of Fe(2+) uptake. Structural basis of novel interactions between the small-GTPase and GDI-like domains in prokaryotic FeoB iron transporter.,Hattori M, Jin Y, Nishimasu H, Tanaka Y, Mochizuki M, Uchiumi T, Ishitani R, Ito K, Nureki O Structure. 2009 Oct 14;17(10):1345-55. Epub 2009 Sep 3. PMID:19733088[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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