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New page: left|200px<br /><applet load="1drm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1drm, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1drm.gif|left|200px]]<br /><applet load="1drm" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1drm, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN==
The FixL proteins are biological oxygen sensors that restrict the, expression of specific genes to hypoxic conditions. FixL's, oxygen-detecting domain is a heme binding region that controls the, activity of an attached histidine kinase. The FixL switch is regulated by, binding of oxygen and other strong-field ligands. In the absence of bound, ligand, the heme domain permits kinase activity. In the presence of bound, ligand, this domain turns off kinase activity. Comparison of the, structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with, bound cyanide, reveals a mechanism of regulation by a heme that is, distinct from the classical hemoglobin models. The close structural, resemblance of the FixL heme domain to the photoactive yellow protein, confirms the existence of a PAS structural motif but reveals the presence, of an alternative regulatory gateway.
<StructureSection load='1drm' size='340' side='right'caption='[[1drm]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1drm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRM 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1drm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drm OCA], [https://pdbe.org/1drm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1drm RCSB], [https://www.ebi.ac.uk/pdbsum/1drm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1drm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FIXL_BRADU FIXL_BRADU] Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ.
== 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/dr/1drm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1drm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The FixL proteins are biological oxygen sensors that restrict the expression of specific genes to hypoxic conditions. FixL's oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. The FixL switch is regulated by binding of oxygen and other strong-field ligands. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity. Comparison of the structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with bound cyanide, reveals a mechanism of regulation by a heme that is distinct from the classical hemoglobin models. The close structural resemblance of the FixL heme domain to the photoactive yellow protein confirms the existence of a PAS structural motif but reveals the presence of an alternative regulatory gateway.


==About this Structure==
Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction.,Gong W, Hao B, Mansy SS, Gonzalez G, Gilles-Gonzalez MA, Chan MK Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15177-82. PMID:9860942<ref>PMID:9860942</ref>
1DRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1BV6. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DRM OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction., Gong W, Hao B, Mansy SS, Gonzalez G, Gilles-Gonzalez MA, Chan MK, Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15177-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9860942 9860942]
</div>
<div class="pdbe-citations 1drm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bradyrhizobium japonicum]]
[[Category: Bradyrhizobium japonicum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chan, M.K.]]
[[Category: Chan MK]]
[[Category: Gilles-Gonzalez, M.A.]]
[[Category: Gilles-Gonzalez MA]]
[[Category: Gong, W.]]
[[Category: Gong W]]
[[Category: Gonzalez, G.]]
[[Category: Gonzalez G]]
[[Category: Hao, B.]]
[[Category: Hao B]]
[[Category: Mansy, S.S.]]
[[Category: Mansy SS]]
[[Category: HEM]]
[[Category: crystal structure]]
[[Category: fixl]]
[[Category: heme domain]]
[[Category: histidine kinase]]
[[Category: pas family]]
[[Category: two-component system]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:31:45 2007''

Latest revision as of 05:46, 13 August 2026

CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN

1drm, resolution 2.40Å

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