2y5y: Difference between revisions

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[[Image:2y5y.jpg|left|200px]]


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==Crystal structure of LacY in complex with an affinity inactivator==
The line below this paragraph, containing "STRUCTURE_2y5y", creates the "Structure Box" on the page.
<StructureSection load='2y5y' size='340' side='right'caption='[[2y5y]], [[Resolution|resolution]] 3.38&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'>[[2y5y]] 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=2Y5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y5Y 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]] 3.38&#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=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=TGA:METHANETHIOSULFONYL-GALACTOSIDE'>TGA</scene></td></tr>
{{STRUCTURE_2y5y|  PDB=2y5y  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5y OCA], [https://pdbe.org/2y5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y5y RCSB], [https://www.ebi.ac.uk/pdbsum/2y5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y5y ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LACY_ECOLI LACY_ECOLI] Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivation more precisely, we solved the structure of single-Cys122 LacY in complex with covalently bound MTS-gal. This structure exhibits an inward-facing conformation similar to that observed previously with a slight narrowing of the cytoplasmic cavity. MTS-gal is bound covalently, forming a disulfide bond with C122 and positioned between R144 and W151. E269, a residue essential for binding, coordinates the C-4 hydroxyl of the galactopyranoside moiety. The location of the sugar is in accord with many biochemical studies.


===CRYSTAL STRUCTURE OF LACY IN COMPLEX WITH AN AFFINITY INACTIVATOR===
Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition.,Chaptal V, Kwon S, Sawaya MR, Guan L, Kaback HR, Abramson J Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9361-6. Epub 2011 May 18. PMID:21593407<ref>PMID:21593407</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2y5y" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_21593407}}, adds the Publication Abstract to the page
*[[Lactose Permease|Lactose Permease]]
(as it appears on PubMed at http://www.pubmed.gov), where 21593407 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_21593407}}
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</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
[[2y5y]] is a 2 chain structure with sequence 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=2Y5Y OCA].
[[Category: Large Structures]]
 
[[Category: Abramson J]]
==Reference==
[[Category: Chaptal V]]
<ref group="xtra">PMID:021593407</ref><ref group="xtra">PMID:012471022</ref><references group="xtra"/>
[[Category: Guan L]]
[[Category: Escherichia coli]]
[[Category: Kaback HR]]
[[Category: Abramson, J.]]
[[Category: Kwon S]]
[[Category: Chaptal, V.]]
[[Category: Sawaya MR]]
[[Category: Guan, L.]]
[[Category: Kaback, H R.]]
[[Category: Kwon, S.]]
[[Category: Sawaya, M R.]]
[[Category: Affinity inactivation]]
[[Category: Transport protein]]

Latest revision as of 13:46, 20 December 2023

Crystal structure of LacY in complex with an affinity inactivatorCrystal structure of LacY in complex with an affinity inactivator

Structural highlights

2y5y 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 3.38Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LACY_ECOLI Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system).

Publication Abstract from PubMed

Lactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivation more precisely, we solved the structure of single-Cys122 LacY in complex with covalently bound MTS-gal. This structure exhibits an inward-facing conformation similar to that observed previously with a slight narrowing of the cytoplasmic cavity. MTS-gal is bound covalently, forming a disulfide bond with C122 and positioned between R144 and W151. E269, a residue essential for binding, coordinates the C-4 hydroxyl of the galactopyranoside moiety. The location of the sugar is in accord with many biochemical studies.

Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition.,Chaptal V, Kwon S, Sawaya MR, Guan L, Kaback HR, Abramson J Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9361-6. Epub 2011 May 18. PMID:21593407[1]

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

See Also

References

  1. Chaptal V, Kwon S, Sawaya MR, Guan L, Kaback HR, Abramson J. Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition. Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9361-6. Epub 2011 May 18. PMID:21593407 doi:10.1073/pnas.1105687108

2y5y, resolution 3.38Å

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