1a3a

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(New page: 200px<br /><applet load="1a3a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a3a, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1a3a.gif|left|200px]]<br /><applet load="1a3a" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a3a, resolution 1.8&Aring;" />
 
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'''CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI==
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BACKGROUND: The bacterial phosphoenolpyruvate-dependent phosphotransferase, system (PTS) catalyses the cellular uptake and subsequent phosphorylation, of carbohydrates. Moreover, the PTS plays a crucial role in the global, regulation of various metabolic pathways. The PTS consists of two general, proteins, enzyme I and the histidine-containing protein (HPr), and the, carbohydrate-specific enzyme II (EII). EIIs are usually composed of two, cytoplasmic domains, IIA and IIB, and a transmembrane domain, IIC. The IIA, domains catalyse the transfer of a phosphoryl group from HPr to IIB, which, phosphorylates the transported carbohydrate. Knowledge of the structures, of the IIA proteins may provide insight into the mechanisms by which the, PTS couples phosphorylation reactions with carbohydrate specificity., RESULTS: We have determined the crystal structure of the Escherichia coli, mannitol-specific IIA domain, IIAmtl (M(r) 16.3 kDa), by multiple, anomalous dispersion analysis of a selenomethionine variant of IIAmtl. The, structure was refined at 1.8 A resolution to an R factor of 19.0% (Rfree, 24.2%). The enzyme consists of a single five-stranded mixed beta sheet, flanked by helices on both sides. The phosphorylation site (His65) is, located at the end of the third beta strand, in a shallow crevice lined, with hydrophobic residues. The sidechains of two conserved active-site, residues, Arg49 and His111, adopt two different conformations in the four, independent IIAmtl molecules. Using a solution structure of phosphorylated, HPr, and a combination of molecular modelling and NMR binding experiments, structural models of the HPr-IIAmtl complex were generated. CONCLUSIONS:, The fold of IIAmtl is completely different from the structures of other, IIA proteins determined so far. The two conformations of Arg49 and His111, might represent different states of the active site, required for the, different phosphoryl transfer reactions in which IIAmtl is involved. A, comparison of the HPr-IIAmtl model with models of HPr in complex with, other IIA enzymes shows that the overall interaction mode between the two, proteins is similar. Differences in the stabilisation of the invariant, residue Arg17 of HPr by the different IIA proteins might be part of a, subtle mechanism to control the hierarchy of carbohydrate utilisation by, the bacterium.
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<StructureSection load='1a3a' size='340' side='right'caption='[[1a3a]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1a3a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A3A FirstGlance]. <br>
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1A3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A3A 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]] 1.8&#8491;</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=1a3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a3a OCA], [https://pdbe.org/1a3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a3a RCSB], [https://www.ebi.ac.uk/pdbsum/1a3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a3a ProSAT]</span></td></tr>
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==Reference==
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</table>
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The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site., van Montfort RL, Pijning T, Kalk KH, Hangyi I, Kouwijzer ML, Robillard GT, Dijkstra BW, Structure. 1998 Mar 15;6(3):377-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9551558 9551558]
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== Function ==
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[[Category: Escherichia coli]]
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[https://www.uniprot.org/uniprot/PTM3C_ECOLI PTM3C_ECOLI] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannitol transport.
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[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
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== Evolutionary Conservation ==
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[[Category: Single protein]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Dijkstra, B.W.]]
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Check<jmol>
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[[Category: Hangyi, I.]]
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<jmolCheckbox>
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[[Category: Kalk, K.H.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a3/1a3a_consurf.spt"</scriptWhenChecked>
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[[Category: Kouwijzer, M.L.C.E.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Montfort, R.L.M.Van.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: Pijning, T.]]
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</jmolCheckbox>
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[[Category: Robillard, G.T.]]
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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=1a3a ConSurf].
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[[Category: histidine phosphorylation]]
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<div style="clear:both"></div>
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[[Category: iia enzymes]]
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__TOC__
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[[Category: phosphoenolpyruvate dependent phosphotransferase system]]
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</StructureSection>
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[[Category: phosphotransferase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:35:07 2007''
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[[Category: Dijkstra BW]]
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[[Category: Hangyi I]]
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[[Category: Kalk KH]]
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[[Category: Kouwijzer MLCE]]
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[[Category: Pijning T]]
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[[Category: Robillard GT]]
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[[Category: Van Montfort RLM]]

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CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI

PDB ID 1a3a

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