2wqx: Difference between revisions

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[[Image:2wqx.png|left|200px]]
==INLB321_4R: S199R, D200R, G206R, A227R, C242A MUTANT OF THE LISTERIA MONOCYTOGENES INLB INTERNALIN DOMAIN==
<StructureSection load='2wqx' size='340' side='right' caption='[[2wqx]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wqx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQX OCA]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h6t|1h6t]], [[1otm|1otm]], [[2uzx|2uzx]], [[1otn|1otn]], [[2uzy|2uzy]], [[1m9s|1m9s]], [[1oto|1oto]], [[1d0b|1d0b]], [[2wqw|2wqw]], [[2wqv|2wqv]], [[2wqu|2wqu]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wqx RCSB], [http://www.ebi.ac.uk/pdbsum/2wqx PDBsum]</span></td></tr>
<table>
== 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/wq/2wqx_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Listeria monocytogenes surface protein InlB mediates bacterial invasion into host cells by activating the human receptor tyrosine kinase Met. So far, it is unknown how InlB or the physiological Met ligand hepatocyte growth factor/scatter factor causes Met dimerization, which is considered a prerequisite for receptor activation. We determined two new structures of InlB, revealing a recurring, antiparallel, dimeric arrangement, in which the two protomers interact through the convex face of the leucine-rich repeat domain. The same contact is found in one structure of the InlB-Met complex. Mutations disrupting the interprotomeric contact of InlB reduced its ability to activate Met and downstream signaling. Conversely, stabilization of this crystal contact by two intermolecular disulfide bonds generates a constitutively dimeric InlB variant with exceptionally high signaling activity, which can stimulate cell motility and cell division. These data demonstrate that the signaling-competent InlB-Met complex assembles with 2:2 stoichiometry around a back-to-back InlB dimer, enabling the direct contact between the stalk region of two Met molecules.


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Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB.,Ferraris DM, Gherardi E, Di Y, Heinz DW, Niemann HH J Mol Biol. 2010 Jan 22;395(3):522-32. Epub 2009 Nov 6. PMID:19900460<ref>PMID:19900460</ref>
The line below this paragraph, containing "STRUCTURE_2wqx", creates the "Structure Box" on the page.
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2wqx|  PDB=2wqx  |  SCENE=  }}


===INLB321_4R: S199R, D200R, G206R, A227R, C242A MUTANT OF THE LISTERIA MONOCYTOGENES INLB INTERNALIN DOMAIN===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
<!--
<references/>
The line below this paragraph, {{ABSTRACT_PUBMED_19900460}}, adds the Publication Abstract to the page
__TOC__
(as it appears on PubMed at http://www.pubmed.gov), where 19900460 is the PubMed ID number.
</StructureSection>
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{{ABSTRACT_PUBMED_19900460}}
 
==About this Structure==
[[2wqx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQX OCA].
 
==Reference==
<ref group="xtra">PMID:019900460</ref><references group="xtra"/>
[[Category: Listeria monocytogenes]]
[[Category: Listeria monocytogenes]]
[[Category: Ferraris, D M.]]
[[Category: Ferraris, D M.]]

Revision as of 11:43, 7 May 2014

INLB321_4R: S199R, D200R, G206R, A227R, C242A MUTANT OF THE LISTERIA MONOCYTOGENES INLB INTERNALIN DOMAININLB321_4R: S199R, D200R, G206R, A227R, C242A MUTANT OF THE LISTERIA MONOCYTOGENES INLB INTERNALIN DOMAIN

Structural highlights

2wqx is a 2 chain structure with sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.
Related:1h6t, 1otm, 2uzx, 1otn, 2uzy, 1m9s, 1oto, 1d0b, 2wqw, 2wqv, 2wqu
Activity:Glucokinase, with EC number 2.7.1.2
Resources:FirstGlance, OCA, RCSB, PDBsum

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

The Listeria monocytogenes surface protein InlB mediates bacterial invasion into host cells by activating the human receptor tyrosine kinase Met. So far, it is unknown how InlB or the physiological Met ligand hepatocyte growth factor/scatter factor causes Met dimerization, which is considered a prerequisite for receptor activation. We determined two new structures of InlB, revealing a recurring, antiparallel, dimeric arrangement, in which the two protomers interact through the convex face of the leucine-rich repeat domain. The same contact is found in one structure of the InlB-Met complex. Mutations disrupting the interprotomeric contact of InlB reduced its ability to activate Met and downstream signaling. Conversely, stabilization of this crystal contact by two intermolecular disulfide bonds generates a constitutively dimeric InlB variant with exceptionally high signaling activity, which can stimulate cell motility and cell division. These data demonstrate that the signaling-competent InlB-Met complex assembles with 2:2 stoichiometry around a back-to-back InlB dimer, enabling the direct contact between the stalk region of two Met molecules.

Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB.,Ferraris DM, Gherardi E, Di Y, Heinz DW, Niemann HH J Mol Biol. 2010 Jan 22;395(3):522-32. Epub 2009 Nov 6. PMID:19900460[1]

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

References

  1. ↑ Ferraris DM, Gherardi E, Di Y, Heinz DW, Niemann HH. Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB. J Mol Biol. 2010 Jan 22;395(3):522-32. Epub 2009 Nov 6. PMID:19900460 doi:10.1016/j.jmb.2009.10.074

2wqx, resolution 2.03Å

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