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1poh

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(New page: 200px<br /><applet load="1poh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1poh, resolution 2.0&Aring;" /> '''THE 2.0 ANGSTROMS RES...)
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[[Image:1poh.jpg|left|200px]]<br /><applet load="1poh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1poh, resolution 2.0&Aring;" />
 
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'''THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION'''<br />
 
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==Overview==
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==THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION==
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The x-ray structure of Escherichia coli HPr has been redetermined at 2.0-A, resolution. In contrast to the previous study (El-Kabbani, O. A. L., Waygood, E. B., and Delbaere, L. T. J. (1987) J. Biol. Chem. 262, 12926-12929), the overall structure is, in general, similar to other, reported NMR and x-ray HPr structures, although there are some important, differences in detail. The overall folding topology of HPr is a classical, open-faced beta-sandwich, consisting of four antiparallel beta-strands and, three alpha-helices. The least square refinement produced an R index of, 0.135 for all measured unique data between 8.0 and 2.0 A resolution. The, active center consists of His15 which is hydrogen bonded to a sulfate, anion, and Arg17 which has a fully open conformation. This corresponds to, the first observed "semi-closed" conformation of the active center of HPr., The Streptococcus faecalis HPr structure (Jia, Z., Vandonselaar, M., Quail, J. W., and Delbaere, L. T. J. (1993) Nature 361, 94-97) has the, "open" conformation in which the side chains of His15 and Arg17 are, directed as far away from each other as possible. The Bacillus subtilis, HPr (Herzberg, O., Reddy, P., Sutrina, S., Saier, M. H., Jr., Reizer, J., and Kapadia, G. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2499-2503) has, the "closed" conformation in which the side chains of His15 and Arg17 are, close together with a sulfate anion located in the active center. The open, conformation represents the unphosphorylated form of HPr whereas the, closed conformation likely resembles the phosphorylated form of HPr. The, semi-closed conformation observed in the E. coli HPr structure could, represent a structural intermediate on the, phosphorylation/dephosphorylation pathway of HPr.
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<StructureSection load='1poh' size='340' side='right'caption='[[1poh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1poh]] is a 1 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=1POH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1POH FirstGlance]. <br>
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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&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1poh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poh OCA], [https://pdbe.org/1poh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1poh RCSB], [https://www.ebi.ac.uk/pdbsum/1poh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1poh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PTHP_ECOLI PTHP_ECOLI] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1poh_consurf.spt"</scriptWhenChecked>
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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=1poh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1POH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1POH OCA].
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*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination., Jia Z, Quail JW, Waygood EB, Delbaere LT, J Biol Chem. 1993 Oct 25;268(30):22490-501. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8226757 8226757]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Delbaere, L.]]
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[[Category: Delbaere L]]
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[[Category: Jia, Z.]]
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[[Category: Jia Z]]
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[[Category: Quail, W.]]
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[[Category: Quail W]]
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[[Category: SO4]]
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[[Category: phosphotransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:58:20 2007''
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Current revision

THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION

PDB ID 1poh

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