1laf: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1laf]] is a 1 chain structure with sequence from [http://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=1LAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAF FirstGlance]. <br> | <table><tr><td colspan='2'>[[1laf]] is a 1 chain structure with sequence from [http://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=1LAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAF FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene></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=1laf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1laf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1laf RCSB], [http://www.ebi.ac.uk/pdbsum/1laf 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=1laf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1laf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1laf RCSB], [http://www.ebi.ac.uk/pdbsum/1laf PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ARGT_SALTY ARGT_SALTY]] This periplasmic binding protein is involved in an arginine transport system. ArgT and histidine-binding protein J (HisJ) interact with a common membrane-bound receptor, HisP. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | [[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | ||
[[Category: Kim, S H | [[Category: Kim, S H]] | ||
[[Category: Oh, B H | [[Category: Oh, B H]] | ||
[[Category: Amino acid transport]] | [[Category: Amino acid transport]] | ||
Revision as of 08:58, 25 December 2014
STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEINSTRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN
Structural highlights
Function[ARGT_SALTY] This periplasmic binding protein is involved in an arginine transport system. ArgT and histidine-binding protein J (HisJ) interact with a common membrane-bound receptor, HisP. 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 substrate-binding site of a protein with multiple specificity should satisfy geometric and energetic complementarity for several different substrates. The structural basis of the multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (LAO) was investigated by determining and analyzing the structures of the protein unliganded and liganded with each of the three high-affinity ligands (L-lysine, L-arginine, and L-ornithine) and with one low-affinity ligand (L-histidine). The geometric complementarity is achieved primarily by virtue of the large size of the ligand-binding site which can accommodate the maximum common volume of the four ligands plus three water molecules. The optimization of energetic complementarity is achieved by the relocation of protein-bound water molecules and by the movement of the Asp-11 side chain. The structure of the LAO-histidine complex indicates that the 30-fold reduced affinity of the protein for histidine is primarily due to unavailability of one ionic interaction of the histidine side chain with the protein which is present in the other three complexes. Structural basis for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein.,Oh BH, Ames GF, Kim SH J Biol Chem. 1994 Oct 21;269(42):26323-30. PMID:7929349[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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