1vlt: Difference between revisions

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<StructureSection load='1vlt' size='340' side='right'caption='[[1vlt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1vlt' size='340' side='right'caption='[[1vlt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1vlt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VLT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1vlt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</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]] 2.2&#8491;</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=1vlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlt OCA], [http://pdbe.org/1vlt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vlt RCSB], [http://www.ebi.ac.uk/pdbsum/1vlt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlt ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></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=1vlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlt OCA], [https://pdbe.org/1vlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlt RCSB], [https://www.ebi.ac.uk/pdbsum/1vlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MCP2_SALTY MCP2_SALTY]] Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.  Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.  
[https://www.uniprot.org/uniprot/MCP2_SALTY MCP2_SALTY] Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.  Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
== 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=1vlt 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=1vlt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The high-resolution structures of the wild-type periplasmic domain of the bacterial aspartate receptor have been determined in the absence and presence of bound aspartate to 1.85 and 2.2 A resolution, respectively. As we reported earlier, in the refined structure of the complexed form of the crosslinked cysteine mutant receptor, the binding of the aspartate at the first site was mediated through four bridging water molecules while the second site showed an occupant electron density that best fit a sulfate group, which was present in the crystallization solution at high concentration. In the wild-type periplasmic domain structure two aspartate residues are bound per dimer, but with different occupancies. There exists a "strong" aspartate-binding site whose binding is again mediated by four water molecules while the second site contains aspartate whose B-factor is about 10% higher, signifying weaker binding. The interaction between the second, "weaker" aspartate with the three ligand-binding arginine side-chains is slightly different from the first site. The major difference is that there are three water molecules mediating the binding of aspartate at the second site, whereas in the first site there are four bridging water molecules. The fact that aspartate-complexed crystals of the wild-type were grown with a large excess aspartate while the cross-linked crystals were grown with equal molar aspartate may explain the difference in the stoichiometry observed. The conservation of the four bridging water molecules in the strong aspartate site of both the cross-linked and wild-type periplasmic domain may reflect an important binding motif. The periplasmic domain in the apo form is a symmetrical dimer, in which each of the subunits is equivalent, and the two aspartate binding sites are identical. Upon the binding of aspartate, the subunits are no longer symmetrical. The main difference between the aspartate-bound and unbound forms is in a small, rigid-body rotation between the subunits within a dimer. The rotation is similar in both direction and magnitude in the crosslinked and wild-type periplasmic domains. The presence of the second aspartate in the wild-type structure does not make any additional rotation compared to the single-site binding. The conservation of the small angular change in vitro suggests that the inter-subunit rotation may have relevance to the understanding of the mechanism of transmembrane signal transduction in vivo.
High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.,Yeh JI, Biemann HP, Prive GG, Pandit J, Koshland DE Jr, Kim SH J Mol Biol. 1996 Sep 20;262(2):186-201. PMID:8831788<ref>PMID:8831788</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1vlt" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Biemann, H P]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Junior, D E.Koshland]]
[[Category: Biemann H-P]]
[[Category: Kim, S H]]
[[Category: Kim S-H]]
[[Category: Pandit, J]]
[[Category: Koshland Junior DE]]
[[Category: Prive, G]]
[[Category: Pandit J]]
[[Category: Yeh, J I]]
[[Category: Prive G]]
[[Category: Bacterial chemotaxis receptor]]
[[Category: Yeh JI]]
[[Category: Bound]]
[[Category: Chemotaxis]]

Latest revision as of 11:46, 14 February 2024

LIGAND BINDING DOMAIN OF THE WILD-TYPE ASPARTATE RECEPTOR WITH ASPARTATELIGAND BINDING DOMAIN OF THE WILD-TYPE ASPARTATE RECEPTOR WITH ASPARTATE

Structural highlights

1vlt is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCP2_SALTY Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis. Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1vlt, resolution 2.20Å

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