View source for 3ezb

==COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI==
<StructureSection load='3ezb' size='340' side='right' caption='[[3ezb]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ezb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ezc 3ezc] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ezd 3ezd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EZB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EZB FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eza|3eza]], [[3eze|3eze]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ezb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ezb OCA], [http://pdbe.org/3ezb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ezb RCSB], [http://www.ebi.ac.uk/pdbsum/3ezb PDBsum]</span></td></tr>
</table>
{{Large structure}}
== Function ==
[[http://www.uniprot.org/uniprot/PT1_ECOLI PT1_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. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).<ref>PMID:7876255</ref>  [[http://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). 
== 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/ez/3ezb_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=3ezb ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer.

Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.,Garrett DS, Seok YJ, Peterkofsky A, Gronenborn AM, Clore GM Nat Struct Biol. 1999 Feb;6(2):166-73. PMID:10048929<ref>PMID:10048929</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ezb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Jmol/Visualizing large molecules|Jmol/Visualizing large molecules]]
*[[Phosphocarrier protein HPr|Phosphocarrier protein HPr]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Phosphoenolpyruvate--protein phosphotransferase]]
[[Category: Clore, G M]]
[[Category: Garrett, D S]]
[[Category: Gronenborn, A M]]
[[Category: Kinase]]
[[Category: Phosphotransferase]]
[[Category: Sugar transport]]
[[Category: Transferase]]