1pw4: Difference between revisions

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<StructureSection load='1pw4' size='340' side='right'caption='[[1pw4]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='1pw4' size='340' side='right'caption='[[1pw4]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pw4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PW4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PW4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PW4 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glpT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 3.3&#8491;</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=1pw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pw4 OCA], [http://pdbe.org/1pw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pw4 RCSB], [http://www.ebi.ac.uk/pdbsum/1pw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pw4 ProSAT]</span></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=1pw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pw4 OCA], [https://pdbe.org/1pw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pw4 RCSB], [https://www.ebi.ac.uk/pdbsum/1pw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pw4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GLPT_ECOLI GLPT_ECOLI]] Responsible for glycerol-3-phosphate uptake.  
[https://www.uniprot.org/uniprot/GLPT_ECOLI GLPT_ECOLI] Responsible for glycerol-3-phosphate uptake.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pw4 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pw4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single-binding site, alternating-access mechanism through a rocker-switch type of movement.
Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli.,Huang Y, Lemieux MJ, Song J, Auer M, Wang DN Science. 2003 Aug 1;301(5633):616-20. PMID:12893936<ref>PMID:12893936</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pw4" style="background-color:#fffaf0;"></div>
==See Also==
*[[Major Facilitators|Major Facilitators]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Auer, M]]
[[Category: Auer M]]
[[Category: Huang, Y]]
[[Category: Huang Y]]
[[Category: Lemieux, M J]]
[[Category: Lemieux MJ]]
[[Category: Song, J]]
[[Category: Song J]]
[[Category: Wang, D N]]
[[Category: Wang DN]]
[[Category: Glycerol-3-phosphate]]
[[Category: Inner membrane]]
[[Category: Major facilitator superfamily]]
[[Category: Membrane protein]]
[[Category: Secondary active membrane transporter]]
[[Category: Transmembrane]]
[[Category: Transporter]]
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