2d4u: Difference between revisions
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[[Image: | ==Crystal Structure of the ligand binding domain of the bacterial serine chemoreceptor Tsr== | ||
<StructureSection load='2d4u' size='340' side='right' caption='[[2d4u]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2d4u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D4U FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2d4u RCSB], [http://www.ebi.ac.uk/pdbsum/2d4u PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/2d4u_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Escherichia coli has closely related amino acid chemoreceptors with distinct ligand specificity: Tar for L-aspartate and Tsr for L-serine. Crystallography of the ligand-binding domain of Tar identified the residues interacting with aspartate, most of which are conserved in Tsr. However, swapping of the non-conserved residues between Tsr and Tar did not change ligand specificity. Analyses with chimeric receptors led us to hypothesize that distinct three-dimensional arrangements of the conserved ligand-binding residues are responsible for ligand specificity. To test this hypothesis, the structures of the apo and serine-binding forms of the ligand-binding domain of Tsr were determined at 1.95 and 2.5 A resolutions, respectively. Some of the Tsr residues are arranged differently from the corresponding aspartate-binding residues of Tar to form a high-affinity serine-binding pocket. The ligand-binding pocket of Tsr was surrounded by negatively charged residues, which presumably exclude negatively charged aspartate molecules. We propose that all these Tsr- and Tar-specific features contribute to specific recognition of serine and aspartate with the arrangement of the side chain of residue 68 (Asn in Tsr and Ser in Tar) being most critical. | |||
Ligand specificity determined by differentially arranged common ligand-binding residues in the bacterial amino acid chemoreceptors Tsr and Tar.,Tajima H, Imada K, Sakuma M, Hattori F, Nara T, Kamo N, Homma M, Kawagishi I J Biol Chem. 2011 Oct 6. PMID:21979954<ref>PMID:21979954</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Chemotaxis protein|Chemotaxis protein]] | |||
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Homma, M.]] | [[Category: Homma, M.]] | ||
