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1drm

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Revision as of 18:33, 10 March 2021

CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN

Structural highlights

1drm is a 1 chain structure. This structure supersedes the now removed PDB entry 1bv6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1bv6, 1bv5, 1dp6, 1dp8, 1dp9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FIXL_BRAJA] 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

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 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.

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^[1]

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

References

↑ Gong W, Hao B, Mansy SS, Gonzalez G, Gilles-Gonzalez MA, Chan MK. Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction. Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15177-82. PMID:9860942

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1drm"

@@ Line 3: / Line 3: @@
 <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. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bv6 1bv6]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1drm]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bv6 1bv6]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bv6|1bv6]], [[1bv5|1bv5]], [[1dp6|1dp6]], [[1dp8|1dp8]], [[1dp9|1dp9]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bv6|1bv6]], [[1bv5|1bv5]], [[1dp6|1dp6]], [[1dp8|1dp8]], [[1dp9|1dp9]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1drm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drm OCA], [http://pdbe.org/1drm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1drm RCSB], [http://www.ebi.ac.uk/pdbsum/1drm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1drm ProSAT]</span></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 ==
-[[http://www.uniprot.org/uniprot/FIXL_BRAJA FIXL_BRAJA]] 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.
+[[https://www.uniprot.org/uniprot/FIXL_BRAJA FIXL_BRAJA]] 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]]

1drm

From Proteopedia

Revision as of 18:33, 10 March 2021

CRYSTAL STRUCTURE OF THE LIGAND FREE BJFIXL HEME DOMAIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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