1hpb

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(New page: 200px<br /><applet load="1hpb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hpb, resolution 2.5&Aring;" /> '''THE BACTERIAL PERIPLA...)
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[[Image:1hpb.gif|left|200px]]<br /><applet load="1hpb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hpb, resolution 2.5&Aring;" />
 
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'''THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS'''<br />
 
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==Overview==
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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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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.
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<StructureSection load='1hpb' size='340' side='right'caption='[[1hpb]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1HPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with HIS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HPB OCA].
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</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>
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<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>
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==Reference==
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<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>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8307974 8307974]
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</table>
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[[Category: Salmonella typhimurium]]
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== Function ==
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[[Category: Single protein]]
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[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.
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[[Category: Kim, S.H.]]
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== Evolutionary Conservation ==
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[[Category: Oh, B.H.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: HIS]]
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Check<jmol>
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[[Category: histidine-binding protein]]
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hp/1hpb_consurf.spt"</scriptWhenChecked>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:43:27 2007''
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1hpb ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Kim SH]]
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[[Category: Oh BH]]

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

PDB ID 1hpb

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