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[[Image:1iib.gif|left|200px]]<br /><applet load="1iib" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1iib, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLI'''<br />


==Overview==
==CRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLI==
BACKGROUND:. The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) mediates the energy-driven uptake of carbohydrates and their concomitant phosphorylation. In addition, the PTS is intimately involved in the regulation of a variety of metabolic and transcriptional processes in the bacterium. The multiprotein PTS consists of a membrane channel and at least four cytoplasmic proteins or protein domains that sequentially transfer a phosphoryl group from phosphoenolpyruvate to the transported carbohydrate. Determination of the three-dimensional structure of the IIB enzymes within the multiprotein complex would provide insights into the mechanisms by which they promote efficient transport by the membrane channel IIC protein and phosphorylate the transported carbohydrate on the inside of the cell. RESULTS:. The crystal structure of the IIB enzyme specific for cellobiose, IIBcellobiose (molecular weight 11.4 kDa), has been determined to a resolution of 1.8 and refined to an R factor of 18.7% (Rfree of 24. 1%). The enzyme consists of a single four-stranded parallel beta sheet flanked by helices on both sides. The phosphorylation site (Cys 10) is located at the C-terminal end of the first beta strand. No positively charged residues, which could assist in phosphoryl-transfer, can be found in or near the active site. The fold of IIBcellobiose is remarkably similar to that of the mammalian low molecular weight protein tyrosine phosphatases. CONCLUSIONS:. A comparison between IIBcellobiose and the structurally similar low molecular weight protein tyrosine phosphatases provides insight into the mechanism of the phosphoryltransfer reactions in which IIBcellobiose is involved. The differences in tertiary structure and active-site composition between IIBcellobiose and the glucose-specific IIBglucose give a structural explanation why the carbo-hydrate-specific components of different families cannot complement each other.
<StructureSection load='1iib' size='340' side='right'caption='[[1iib]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1iib]] is a 2 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=1IIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IIB FirstGlance]. <br>
1IIB 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] Known structural/functional Site: <scene name='pdbsite=1:CYS+10+Is+The+Phosphorylation+Site+In+The+Active+Protein'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIB 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]] 1.8&#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=1iib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iib OCA], [https://pdbe.org/1iib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iib RCSB], [https://www.ebi.ac.uk/pdbsum/1iib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iib ProSAT]</span></td></tr>
==Reference==
</table>
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases., van Montfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Thunnissen MM, Robillard GT, Dijkstra BW, Structure. 1997 Feb 15;5(2):217-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9032081 9032081]
== Function ==
[[Category: Escherichia coli]]
[https://www.uniprot.org/uniprot/PTQB_ECOLI PTQB_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 N,N'-diacetylchitobiose transport.<ref>PMID:10913117</ref>
[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
== Evolutionary Conservation ==
[[Category: Single protein]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Dijkstra, B W.]]
Check<jmol>
[[Category: Kalk, K H.]]
  <jmolCheckbox>
[[Category: Montfort, R L.M Van.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ii/1iib_consurf.spt"</scriptWhenChecked>
[[Category: Pijning, T.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Reizer, J.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Robillard, G T.]]
  </jmolCheckbox>
[[Category: Saier, M H.]]
</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=1iib ConSurf].
[[Category: Thunnissen, M M.G M.]]
<div style="clear:both"></div>
[[Category: cysteine phosphorylation]]
== References ==
[[Category: iib enzymes]]
<references/>
[[Category: phosphoenolpyruvate dependent phosphotransferase system]]
__TOC__
[[Category: phosphotransferase]]
</StructureSection>
 
[[Category: Escherichia coli K-12]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:12 2008''
[[Category: Large Structures]]
[[Category: Dijkstra BW]]
[[Category: Kalk KH]]
[[Category: Pijning T]]
[[Category: Reizer J]]
[[Category: Robillard GT]]
[[Category: Saier MH]]
[[Category: Thunnissen MMGM]]
[[Category: Van Montfort RLM]]

Latest revision as of 10:35, 7 February 2024

CRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLICRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLI

Structural highlights

1iib is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTQB_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 N,N'-diacetylchitobiose transport.[1]

Evolutionary Conservation

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

References

  1. ↑ Keyhani NO, Wang LX, Lee YC, Roseman S. The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J Biol Chem. 2000 Oct 20;275(42):33084-90. PMID:10913117 doi:http://dx.doi.org/10.1074/jbc.M001043200

1iib, resolution 1.80Å

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