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[[Image:1e2a.gif|left|200px]]


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==ENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTIS==
The line below this paragraph, containing "STRUCTURE_1e2a", creates the "Structure Box" on the page.
<StructureSection load='1e2a' size='340' side='right'caption='[[1e2a]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1e2a]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E2A FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1e2a|  PDB=1e2a  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2a OCA], [https://pdbe.org/1e2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e2a RCSB], [https://www.ebi.ac.uk/pdbsum/1e2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2a ProSAT]</span></td></tr>
 
</table>
'''ENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTIS'''
== Function ==
 
[https://www.uniprot.org/uniprot/PTLA_LACLL PTLA_LACLL] The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in lactose transport.
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
BACKGROUND: The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is responsible for the binding, transmembrane transport and phosphorylation of numerous sugar substrates. The system is also involved in the regulation of a variety of metabolic and transcriptional processes. The PTS consists of two non-specific energy coupling components, enzyme I and a heat stable phosphocarrier protein (HPr), as well as several sugar-specific multiprotein permeases known as enzymes II. In most cases, enzymes IIA and IIB are located in the cytoplasm, while enzyme IIC acts as a membrane channel. Enzyme IIAlactose belongs to the lactose/cellobiose-specific family of enzymes II, one of four functionally and structurally distinct groups. The protein, which normally functions as a trimer, is believed to separate into its subunits after phosphorylation. RESULTS: The crystal structure of the trimeric enzyme IIAlactose from Lactococcus lactis has been determined at 2.3 A resolution. The subunits of the enzyme, related to each other by the inherent threefold rotational symmetry, possess interesting structural features such as coiled-coil-like packing and a methionine cluster. The subunits each comprise three helices (I, II and III) and pack against each other forming a nine-helix bundle. This helical bundle is stabilized by a centrally located metal ion and also encloses a hydrophobic cavity. The three phosphorylation sites (His78 on each monomer) are located in helices III and their sidechains protrude into a large groove between helices I and II of the neighbouring subunits. A model of the complex between phosphorylated HPr and enzyme IIAlactose has been constructed. CONCLUSIONS: Enzyme IIAlactose is the first representative of the family of lactose/cellobiose-specific enzymes IIA for which a three-dimensional structure has been determined. Some of its structural features, like the presence of two histidine residues at the active site, seem to be common to all enzymes no overall structural homology is observed to any PTS proteins or to any other proteins in the Protein Data Bank. Enzyme IIAlactose shows surface complementarity to the phosphorylated form of HPr and several energetically favourable interactions between the two molecules can be predicted.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/1e2a_consurf.spt"</scriptWhenChecked>
1E2A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2A OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system., Sliz P, Engelmann R, Hengstenberg W, Pai EF, Structure. 1997 Jun 15;5(6):775-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9261069 9261069]
</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=1e2a ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Engelmann, R.]]
[[Category: Engelmann R]]
[[Category: Hengstenberg, W.]]
[[Category: Hengstenberg W]]
[[Category: Pai, E F.]]
[[Category: Pai EF]]
[[Category: Sliz, P.]]
[[Category: Sliz P]]
[[Category: Enzyme iia]]
[[Category: Helical bundle]]
[[Category: Phosphotransferase system]]
[[Category: Pt]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:34:14 2008''

Latest revision as of 10:00, 7 February 2024

ENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTISENZYME IIA FROM THE LACTOSE SPECIFIC PTS FROM LACTOCOCCUS LACTIS

Structural highlights

1e2a is a 3 chain structure with sequence from Lactococcus lactis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTLA_LACLL The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in lactose transport.

Evolutionary Conservation

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

1e2a, resolution 2.30Å

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