1vrc

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(New page: 200px<br /><applet load="1vrc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vrc" /> '''Complex of enzyme IIAmannose and the histidi...)
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'''Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure'''<br />
 
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==Overview==
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==Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure==
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The solution structure of the 48-kDa IIA(Man)-HPr complex of the mannose, branch of the Escherichia coli phosphotransferase system has been solved, by NMR using conjoined rigid body/torsion angle-simulated annealing on the, basis of intermolecular nuclear Overhauser enhancement data and residual, dipolar couplings. IIA(Man) is dimeric and has two symmetrically related, binding sites per dimer for HPr. A convex surface on HPr, formed primarily, by helices 1 and 2, interacts with a deep groove at the interface of the, two subunits of IIA(Man). The interaction surface on IIA(Man) is, predominantly helical, comprising helix 3 from the subunit that bears the, active site His-10 and helices 1, 4, and 5 from the other subunit. The, total buried accessible surface area at the protein-protein interface is, 1450 A(2). The binding sites on the two proteins are complementary in, terms of shape and distribution of hydrophobic, hydrophilic, and charged, residues. The active site histidines, His-10 of IIA(Man) and His-15, (italics indicate HPr residues) of HPr, are in close proximity. An, associative transition state involving a pentacoordinate phosphoryl group, with trigonal bipyramidal geometry bonded to the N-epsilon2 atom of His-10, and the N-delta1 atom of His-15 can be readily formed with negligible, displacement in the backbone coordinates of the residues immediately, adjacent to the active site histidines. Comparing the structures of, complexes of HPr with three other structurally unrelated, phosphotransferase system proteins, enzymes I, IIA(glucose), and, IIA(mannitol), reveals a number of common features that provide a, molecular basis for understanding how HPr specifically recognizes a wide, range of diverse proteins.
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<StructureSection load='1vrc' size='340' side='right'caption='[[1vrc]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vrc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VRC 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">Solution NMR</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=PO3:PHOSPHITE+ION'>PO3</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=1vrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrc OCA], [https://pdbe.org/1vrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vrc RCSB], [https://www.ebi.ac.uk/pdbsum/1vrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vrc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PTNAB_ECOLI PTNAB_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 mannose transport.
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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/vr/1vrc_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=1vrc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The solution structure of the 48-kDa IIA(Man)-HPr complex of the mannose branch of the Escherichia coli phosphotransferase system has been solved by NMR using conjoined rigid body/torsion angle-simulated annealing on the basis of intermolecular nuclear Overhauser enhancement data and residual dipolar couplings. IIA(Man) is dimeric and has two symmetrically related binding sites per dimer for HPr. A convex surface on HPr, formed primarily by helices 1 and 2, interacts with a deep groove at the interface of the two subunits of IIA(Man). The interaction surface on IIA(Man) is predominantly helical, comprising helix 3 from the subunit that bears the active site His-10 and helices 1, 4, and 5 from the other subunit. The total buried accessible surface area at the protein-protein interface is 1450 A(2). The binding sites on the two proteins are complementary in terms of shape and distribution of hydrophobic, hydrophilic, and charged residues. The active site histidines, His-10 of IIA(Man) and His-15 (italics indicate HPr residues) of HPr, are in close proximity. An associative transition state involving a pentacoordinate phosphoryl group with trigonal bipyramidal geometry bonded to the N-epsilon2 atom of His-10 and the N-delta1 atom of His-15 can be readily formed with negligible displacement in the backbone coordinates of the residues immediately adjacent to the active site histidines. Comparing the structures of complexes of HPr with three other structurally unrelated phosphotransferase system proteins, enzymes I, IIA(glucose), and IIA(mannitol), reveals a number of common features that provide a molecular basis for understanding how HPr specifically recognizes a wide range of diverse proteins.
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==About this Structure==
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Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system.,Williams DC Jr, Cai M, Suh JY, Peterkofsky A, Clore GM J Biol Chem. 2005 May 27;280(21):20775-84. Epub 2005 Mar 23. PMID:15788390<ref>PMID:15788390</ref>
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1VRC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1VRC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system., Williams DC Jr, Cai M, Suh JY, Peterkofsky A, Clore GM, J Biol Chem. 2005 May 27;280(21):20775-84. Epub 2005 Mar 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15788390 15788390]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1vrc" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
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[[Category: Clore, G.M.]]
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[[Category: Williams, D.C.]]
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[[Category: complex (transferase/phosphocarrier)]]
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[[Category: kinase]]
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[[Category: phosphotransferase]]
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[[Category: sugar transport]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:05:23 2007''
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==See Also==
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*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Clore GM]]
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[[Category: Williams DC]]

Current revision

Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure

PDB ID 1vrc

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