1hsl: Difference between revisions

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<StructureSection load='1hsl' size='340' side='right'caption='[[1hsl]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
<StructureSection load='1hsl' size='340' side='right'caption='[[1hsl]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hsl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HSL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1hsl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HSL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</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]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</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=1hsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsl OCA], [https://pdbe.org/1hsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hsl RCSB], [https://www.ebi.ac.uk/pdbsum/1hsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hsl ProSAT]</span></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=1hsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsl OCA], [https://pdbe.org/1hsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hsl RCSB], [https://www.ebi.ac.uk/pdbsum/1hsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hsl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HISJ_ECOLI HISJ_ECOLI]] Component of the high-affinity histidine permease, a binding-protein-dependent transport system. The other components are proteins HisQ, HisM, and HisP.  
[https://www.uniprot.org/uniprot/HISJ_ECOLI HISJ_ECOLI] Component of the high-affinity histidine permease, a binding-protein-dependent transport system. The other components are proteins HisQ, HisM, and HisP.
== 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=1hsl 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=1hsl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the histidine-binding protein (HBP, M(r) = 26,100), involved solely in active transport, has been determined by the molecular replacement technique and refined to 1.89-A resolution and to an R-factor of 0.199. The structure is that of two protein molecules, each with a bound L-histidine, in the asymmetric unit. Replacement solution was achieved by using a model of the crystal structure of the ligand-free, open-cleft form of the lysine/arginine/ornithine-binding protein which was modified so that the two domains are close to each other by bending the hinge connecting the two domains. The bound histidine is held in place by 10 hydrogen bonds, 2 salt links, and about 60 van der Waals contacts. Elucidation of the HBP structure brings a total of eight different binding proteins structures determined in our laboratory, including those with specificities for monosaccharides, maltodextrins (linear and cyclic), aliphatic amino acids, and inorganic oxyanions. These structures comprise about a third of the entire family of periplasmic binding proteins which act as initial primary high-affinity receptors of active transport in Gram-negative bacteria. Two of the binding proteins with specificities for glucose/galactose and maltodextrins also serve in a similar capacity in chemotaxis. Though these proteins have different molecular weights (ranging from 26,000 to 40,000), amino acid sequences, and ligand specificities, their three-dimensional structures are similar overall. They are elongated (axial ratios of 2:1) and composed of two similar globular domains separated by a deep cleft wherein the ligand-binding site is located. These structures provide understanding of molecular recognition of a variety of ligands at the atomic level and functional roles of the binding proteins.
Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins.,Yao N, Trakhanov S, Quiocho FA Biochemistry. 1994 Apr 26;33(16):4769-79. PMID:8161536<ref>PMID:8161536</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hsl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Quiocho, F A]]
[[Category: Quiocho FA]]
[[Category: Trakhanov, S]]
[[Category: Trakhanov S]]
[[Category: Yao, N]]
[[Category: Yao N]]
[[Category: Binding protein]]

Revision as of 14:34, 27 March 2024

REFINED 1.89 ANGSTROMS STRUCTURE OF THE HISTIDINE-BINDING PROTEIN COMPLEXED WITH HISTIDINE AND ITS RELATIONSHIP WITH MANY OTHER ACTIVE TRANSPORT(SLASH)CHEMOSENSORY RECEPTORSREFINED 1.89 ANGSTROMS STRUCTURE OF THE HISTIDINE-BINDING PROTEIN COMPLEXED WITH HISTIDINE AND ITS RELATIONSHIP WITH MANY OTHER ACTIVE TRANSPORT(SLASH)CHEMOSENSORY RECEPTORS

Structural highlights

1hsl is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.89Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HISJ_ECOLI Component of the high-affinity histidine permease, a binding-protein-dependent transport system. The other components are proteins HisQ, HisM, and HisP.

Evolutionary Conservation

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

1hsl, resolution 1.89Å

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OCA
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