1pdo: Difference between revisions

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New page: left|200px<br /><applet load="1pdo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pdo, resolution 1.7Å" /> '''PHOSPHOENOLPYRUVATE-D...
 
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'''PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM'''<br />


==Overview==
==PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM==
The mannose transporter from Escherichia coli is a member of the, phosphoenolpyruvate-dependent phosphotransferase system. The multi-subunit, complex couples translocation across the bacterial inner membrane with, phosphorylation of the solute. A functional fragment (IIA(Man), residues 2, to 133) of the membrane-associated IIAB(Man) subunit of the mannose, transporter was expressed as a selenomethionine protein, and the, unphosphorylated molecule was crystallized and its structure solved by, X-ray crystallography. The protein consists of a central five-stranded, beta-sheet covered by helices on either face. The order of the secondary, structure elements is (beta alpha)4, alpha beta. Four beta-strands are, arranged in a parallel manner with strand order 2134 and are linked by, helices forming right-handed cross-over connections. The fifth strand that, forms one edge of the sheet and runs antiparallel to the others is swapped, between the subunits of the dimeric structure. Helices D and E form a, helical hairpin. Histidine 10, which is transiently phosphorylated during, catalysis, is located at the topological switch-point of the structure, close to the subunit interface. Its imidazole ring is hydrogen bonded to, the buried side-chain of Asp67. It is likely that Asp67 acts as a general, base and thus increases the nucleophilicity of the histidine. Modeling, suggests that the covalently bound phosphoryl group would be stabilized by, the macrodipole of helix C. Putative interactions between IIA(Man) and the, histidine-containing phosphocarrier protein are discussed.
<StructureSection load='1pdo' size='340' side='right'caption='[[1pdo]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1pdo]] 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=1PDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PDO FirstGlance]. <br>
1PDO 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=1PDO OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=1pdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pdo OCA], [https://pdbe.org/1pdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pdo RCSB], [https://www.ebi.ac.uk/pdbsum/1pdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pdo ProSAT]</span></td></tr>
==Reference==
</table>
Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution., Nunn RS, Markovic-Housley Z, Genovesio-Taverne JC, Flukiger K, Rizkallah PJ, Jansonius JN, Schirmer T, Erni B, J Mol Biol. 1996 Jun 14;259(3):502-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8676384 8676384]
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pd/1pdo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1pdo ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Erni B]]
[[Category: Erni, B.]]
[[Category: Nunn RS]]
[[Category: Nunn, R.S.]]
[[Category: Schirmer T]]
[[Category: Schirmer, T.]]
[[Category: phosphoenolpyruvate dependent phosphotransferase system]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:43:10 2007''

Latest revision as of 11:07, 14 February 2024

PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEMPHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM

Structural highlights

1pdo is a 1 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 1.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

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

1pdo, resolution 1.70Å

Drag the structure with the mouse to rotate

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