3l6h: Difference between revisions

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[[Image:3l6h.jpg|left|200px]]


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==Crystal structure of lactococcal OpuAC in its closed-liganded conformation complexed with glycine betaine==
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<StructureSection load='3l6h' size='340' side='right'caption='[[3l6h]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3l6h]] is a 1 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=3L6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L6H FirstGlance]. <br>
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</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=BET:TRIMETHYL+GLYCINE'>BET</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
{{STRUCTURE_3l6h|  PDB=3l6h  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6h OCA], [https://pdbe.org/3l6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l6h RCSB], [https://www.ebi.ac.uk/pdbsum/3l6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7DAU8_LACLA Q7DAU8_LACLA]
== 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/l6/3l6h_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=3l6h ConSurf].
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== Publication Abstract from PubMed ==
BACKGROUND: The ABC transporter OpuA from Lactococcus lactis transports glycine betaine upon activation by threshold values of ionic strength. In this study, the ligand binding characteristics of purified OpuA in a detergent-solubilized state and of its substrate-binding domain produced as soluble protein (OpuAC) was characterized. PRINCIPAL FINDINGS: The binding of glycine betaine to purified OpuA and OpuAC (K(D) = 4-6 microM) did not show any salt dependence or cooperative effects, in contrast to the transport activity. OpuAC is highly specific for glycine betaine and the related proline betaine. Other compatible solutes like proline and carnitine bound with affinities that were 3 to 4 orders of magnitude lower. The low affinity substrates were not noticeably transported by membrane-reconstituted OpuA. OpuAC was crystallized in an open (1.9 A) and closed-liganded (2.3 A) conformation. The binding pocket is formed by three tryptophans (Trp-prism) coordinating the quaternary ammonium group of glycine betaine in the closed-liganded structure. Even though the binding site of OpuAC is identical to that of its B. subtilis homolog, the affinity for glycine betaine is 4-fold higher. CONCLUSIONS: Ionic strength did not affect substrate binding to OpuA, indicating that regulation of transport is not at the level of substrate binding, but rather at the level of translocation. The overlap between the crystal structures of OpuAC from L.lactis and B.subtilis, comprising the classical Trp-prism, show that the differences observed in the binding affinities originate from outside of the ligand binding site.


===Crystal structure of lactococcal OpuAC in its closed-liganded conformation complexed with glycine betaine===
Ligand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA.,Wolters JC, Berntsson RP, Gul N, Karasawa A, Thunnissen AM, Slotboom DJ, Poolman B PLoS One. 2010 Apr 29;5(4):e10361. PMID:20454456<ref>PMID:20454456</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3l6h" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20454456 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_20454456}}
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</StructureSection>
==About this Structure==
3L6H is a 1 chain structure with 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=3L6H OCA].
 
==Reference==
<ref group="xtra">PMID:20454456</ref><references group="xtra"/>
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
[[Category: Berntsson, R P.A.]]
[[Category: Large Structures]]
[[Category: Gul, N.]]
[[Category: Berntsson RPA]]
[[Category: Karasawa, A.]]
[[Category: Gul N]]
[[Category: Poolman, B.]]
[[Category: Karasawa A]]
[[Category: Slotboom, D J.]]
[[Category: Poolman B]]
[[Category: Thunnissen, A M.W H.]]
[[Category: Slotboom DJ]]
[[Category: Wolters, J C.]]
[[Category: Thunnissen AMWH]]
[[Category: Cell membrane]]
[[Category: Wolters JC]]
[[Category: Glycine betaine binding]]
[[Category: Glycine betaine-binding protein]]
[[Category: Membrane]]
[[Category: Substrate binding domain]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Venus fly-trap]]
 
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