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1hpb

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THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS

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Retrieved from "http://52.214.119.220/wiki/index.php/1hpb"

Categories: Large Structures | Salmonella enterica subsp. enterica serovar Typhimurium | Kim SH | Oh BH

@@ Line 1: / Line 1: @@
-[[Image:1hpb.gif|left|200px]]
- {{Structure
+==THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS==
-|PDB= 1hpb |SIZE=350|CAPTION= <scene name='initialview01'>1hpb</scene>, resolution 2.5&Aring;
+<StructureSection load='1hpb' size='340' side='right'caption='[[1hpb]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>
+<table><tr><td colspan='2'>[[1hpb]] is a 1 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=1HPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HPB FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpb OCA], [https://pdbe.org/1hpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hpb RCSB], [https://www.ebi.ac.uk/pdbsum/1hpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hpb ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpb OCA], [http://www.ebi.ac.uk/pdbsum/1hpb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hpb RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/HISJ_SALTY HISJ_SALTY] Component of the high-affinity histidine permease, a binding-protein-dependent transport system. The other components are proteins HisQ, HisM, and HisP.
+== Evolutionary Conservation ==
-'''THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hp/1hpb_consurf.spt"</scriptWhenChecked>
-Bacterial periplasmic binding proteins are initial receptors in the process of active transport across cell membranes and/or chemotaxis. Among them, the histidine-binding protein (HisJ) has been extensively studied from the biochemical, physiological, and genetic points of view. The three-dimensional crystal structure of the histidine-binding protein complexed with histidine has been determined at 2.5-A resolution by the molecular replacement method using a probe structure the previously solved lysine-liganded structure of the lysine-, arginine-, ornithine-binding protein (LAO), which shares 70% sequence identity with HisJ. The structure is bi-lobate; the two lobes, one bigger than the other, are connected by two short strands and are in contact with each other (closed) enclosing the histidine. Charged, polar, and non-polar side chains, as well as the peptide backbone, are involved in tight binding of the histidine. The bound histidine is involved in eight direct hydrogen bonds, six with the bigger lobe and two with the smaller lobe, in one potential water-mediated hydrogen bond with the bigger lobe, as well as in ionic interactions. The HisJ residues surrounding the ligand are the same as the LAO residues interacting with lysine, except for residue 52 which is leucine in HisJ and phenylalanine in LAO. The Leu-52 in HisJ makes a hydrophobic interaction with the imidazole ring of histidine. Of seven mutations affecting the ligand-binding site, five are located in the ligand-binding site, one in a connecting strand, and one at the domains interface. Based on comparisons among related binding proteins, the specific interactions between the ligands and the respective binding protein residues are predicted for the glutamine-binding protein and the opines-binding protein.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-HPB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPB OCA].
+</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=1hpb ConSurf].
+<div style="clear:both"></div>
-==Reference==
+__TOC__
-The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins., Oh BH, Kang CH, De Bondt H, Kim SH, Nikaido K, Joshi AK, Ames GF, J Biol Chem. 1994 Feb 11;269(6):4135-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8307974 8307974]
+</StructureSection>
-[[Category: Salmonella typhimurium]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-[[Category: Kim, S H.]]
+[[Category: Kim SH]]
-[[Category: Oh, B H.]]
+[[Category: Oh BH]]
-[[Category: histidine-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:36 2008''

1hpb

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Current revision

THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS

Structural highlights

Function

Evolutionary Conservation

Contents

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