3bp8: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_3bp8", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3bp8.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_3bp8", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_3bp8|  PDB=3bp8  |  SCENE=  }}
'''Crystal structure of Mlc/EIIB complex'''


==Crystal structure of Mlc/EIIB complex==
<StructureSection load='3bp8' size='340' side='right'caption='[[3bp8]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bp8]] is a 4 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=3BP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BP8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3bp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bp8 OCA], [https://pdbe.org/3bp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bp8 RCSB], [https://www.ebi.ac.uk/pdbsum/3bp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bp8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MLC_ECOLI MLC_ECOLI] Transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. Regulates the expression of malT.<ref>PMID:10464268</ref> <ref>PMID:11361067</ref>
== 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/bp/3bp8_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=3bp8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Escherichia coli, glucose-dependent transcriptional induction of genes encoding a variety of sugar-metabolizing enzymes and transport systems is mediated by the phosphorylation state-dependent interaction of membrane-bound enzyme IICB(Glc) (EIICB(Glc)) with the global repressor Mlc. Here we report the crystal structure of a tetrameric Mlc in a complex with four molecules of enzyme IIB(Glc) (EIIB), the cytoplasmic domain of EIICB(Glc). Each monomer of Mlc has one bound EIIB molecule, indicating the 1:1 stoichiometry. The detailed view of the interface, along with the high-resolution structure of EIIB containing a sulfate ion at the phosphorylation site, suggests that the phosphorylation-induced steric hindrance and disturbance of polar intermolecular interactions impede complex formation. Furthermore, we reveal that Mlc possesses a built-in flexibility for the structural adaptation to its target DNA and that interaction of Mlc with EIIB fused only to dimeric proteins resulted in the loss of its DNA binding ability, suggesting that flexibility of the Mlc structure is indispensable for its DNA binding.


==Overview==
Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration.,Nam TW, Jung HI, An YJ, Park YH, Lee SH, Seok YJ, Cha SS Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3751-6. Epub 2008 Mar 4. PMID:18319344<ref>PMID:18319344</ref>
In Escherichia coli, glucose-dependent transcriptional induction of genes encoding a variety of sugar-metabolizing enzymes and transport systems is mediated by the phosphorylation state-dependent interaction of membrane-bound enzyme IICB(Glc) (EIICB(Glc)) with the global repressor Mlc. Here we report the crystal structure of a tetrameric Mlc in a complex with four molecules of enzyme IIB(Glc) (EIIB), the cytoplasmic domain of EIICB(Glc). Each monomer of Mlc has one bound EIIB molecule, indicating the 1:1 stoichiometry. The detailed view of the interface, along with the high-resolution structure of EIIB containing a sulfate ion at the phosphorylation site, suggests that the phosphorylation-induced steric hindrance and disturbance of polar intermolecular interactions impede complex formation. Furthermore, we reveal that Mlc possesses a built-in flexibility for the structural adaptation to its target DNA and that interaction of Mlc with EIIB fused only to dimeric proteins resulted in the loss of its DNA binding ability, suggesting that flexibility of the Mlc structure is indispensable for its DNA binding.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
3BP8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BP8 OCA].
</div>
<div class="pdbe-citations 3bp8" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration., Nam TW, Jung HI, An YJ, Park YH, Lee SH, Seok YJ, Cha SS, Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3751-6. Epub 2008 Mar 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18319344 18319344]
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: An, Y J.]]
[[Category: An YJ]]
[[Category: Cha, S S.]]
[[Category: Cha SS]]
[[Category: Jung, H I.]]
[[Category: Jung HI]]
[[Category: Enzyme]]
[[Category: Glucose signaling]]
[[Category: Iicbglc]]
[[Category: Inner membrane]]
[[Category: Kinase]]
[[Category: Membrane]]
[[Category: Mlc]]
[[Category: Phosphoprotein]]
[[Category: Phosphotransferase system]]
[[Category: Protein-protein interaction]]
[[Category: Sugar transport]]
[[Category: Transcription regulation]]
[[Category: Transferase]]
[[Category: Transmembrane]]
[[Category: Transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:19:55 2008''

Latest revision as of 17:49, 1 November 2023

Crystal structure of Mlc/EIIB complexCrystal structure of Mlc/EIIB complex

Structural highlights

3bp8 is a 4 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 2.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MLC_ECOLI Transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. Regulates the expression of malT.[1] [2]

Evolutionary Conservation

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

Publication Abstract from PubMed

In Escherichia coli, glucose-dependent transcriptional induction of genes encoding a variety of sugar-metabolizing enzymes and transport systems is mediated by the phosphorylation state-dependent interaction of membrane-bound enzyme IICB(Glc) (EIICB(Glc)) with the global repressor Mlc. Here we report the crystal structure of a tetrameric Mlc in a complex with four molecules of enzyme IIB(Glc) (EIIB), the cytoplasmic domain of EIICB(Glc). Each monomer of Mlc has one bound EIIB molecule, indicating the 1:1 stoichiometry. The detailed view of the interface, along with the high-resolution structure of EIIB containing a sulfate ion at the phosphorylation site, suggests that the phosphorylation-induced steric hindrance and disturbance of polar intermolecular interactions impede complex formation. Furthermore, we reveal that Mlc possesses a built-in flexibility for the structural adaptation to its target DNA and that interaction of Mlc with EIIB fused only to dimeric proteins resulted in the loss of its DNA binding ability, suggesting that flexibility of the Mlc structure is indispensable for its DNA binding.

Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration.,Nam TW, Jung HI, An YJ, Park YH, Lee SH, Seok YJ, Cha SS Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3751-6. Epub 2008 Mar 4. PMID:18319344[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kim SY, Nam TW, Shin D, Koo BM, Seok YJ, Ryu S. Purification of Mlc and analysis of its effects on the pts expression in Escherichia coli. J Biol Chem. 1999 Sep 3;274(36):25398-402. PMID:10464268
  2. ↑ Plumbridge J. Regulation of PTS gene expression by the homologous transcriptional regulators, Mlc and NagC, in Escherichia coli (or how two similar repressors can behave differently). J Mol Microbiol Biotechnol. 2001 Jul;3(3):371-80. PMID:11361067
  3. ↑ Nam TW, Jung HI, An YJ, Park YH, Lee SH, Seok YJ, Cha SS. Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration. Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3751-6. Epub 2008 Mar 4. PMID:18319344

3bp8, resolution 2.85Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3bp8&oldid=3931831"