4f35: Difference between revisions

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==Crystal Structure of a bacterial dicarboxylate/sodium symporter==
==Crystal Structure of a bacterial dicarboxylate/sodium symporter==
<StructureSection load='4f35' size='340' side='right' caption='[[4f35]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='4f35' size='340' side='right'caption='[[4f35]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4f35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F35 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4f35]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F35 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 3.196&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VC_A0025 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</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=4f35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f35 OCA], [https://pdbe.org/4f35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f35 RCSB], [https://www.ebi.ac.uk/pdbsum/4f35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f35 ProSAT]</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=4f35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f35 OCA], [http://pdbe.org/4f35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f35 RCSB], [http://www.ebi.ac.uk/pdbsum/4f35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f35 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9KNE0_VIBCH Q9KNE0_VIBCH]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4f35" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4f35" style="background-color:#fffaf0;"></div>
==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillo virgola del koch trevisan 1884]]
[[Category: Large Structures]]
[[Category: Gregorio, G G]]
[[Category: Vibrio cholerae]]
[[Category: Liu, Q]]
[[Category: Gregorio GG]]
[[Category: Mancusso, R L]]
[[Category: Liu Q]]
[[Category: Wang, D N]]
[[Category: Mancusso RL]]
[[Category: Transport protein]]
[[Category: Wang DN]]
[[Category: Transporter]]

Latest revision as of 09:30, 17 October 2024

Crystal Structure of a bacterial dicarboxylate/sodium symporterCrystal Structure of a bacterial dicarboxylate/sodium symporter

Structural highlights

4f35 is a 4 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.196Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9KNE0_VIBCH

Publication Abstract from PubMed

In human cells, cytosolic citrate is a chief precursor for the synthesis of fatty acids, triacylglycerols, cholesterol and low-density lipoprotein. Cytosolic citrate further regulates the energy balance of the cell by activating the fatty-acid-synthesis pathway while downregulating both the glycolysis and fatty-acid beta-oxidation pathways. The rate of fatty-acid synthesis in liver and adipose cells, the two main tissue types for such synthesis, correlates directly with the concentration of citrate in the cytosol, with the cytosolic citrate concentration partially depending on direct import across the plasma membrane through the Na(+)-dependent citrate transporter (NaCT). Mutations of the homologous fly gene (Indy; I'm not dead yet) result in reduced fat storage through calorie restriction. More recently, Nact (also known as Slc13a5)-knockout mice have been found to have increased hepatic mitochondrial biogenesis, higher lipid oxidation and energy expenditure, and reduced lipogenesis, which taken together protect the mice from obesity and insulin resistance. To understand the transport mechanism of NaCT and INDY proteins, here we report the 3.2 A crystal structure of a bacterial INDY homologue. One citrate molecule and one sodium ion are bound per protein, and their binding sites are defined by conserved amino acid motifs, forming the structural basis for understanding the specificity of the transporter. Comparison of the structures of the two symmetrical halves of the transporter suggests conformational changes that propel substrate translocation.

Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter.,Mancusso R, Gregorio GG, Liu Q, Wang DN Nature. 2012 Nov 22;491(7425):622-6. doi: 10.1038/nature11542. Epub 2012 Oct 21. PMID:23086149[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Mancusso R, Gregorio GG, Liu Q, Wang DN. Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter. Nature. 2012 Nov 22;491(7425):622-6. doi: 10.1038/nature11542. Epub 2012 Oct 21. PMID:23086149 doi:http://dx.doi.org/10.1038/nature11542

4f35, resolution 3.20Å

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OCA