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2vuh

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Revision as of 14:21, 5 August 2016

CRYSTAL STRUCTURE OF THE D55E MUTANT OF THE HUPR RECEIVER DOMAIN

Structural highlights

2vuh is a 1 chain structure with sequence from "rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2jk1, 2vui
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HUPR_RHOCA] Probable member of the two-component regulatory system involved in the regulation of the [NiFe] hydrogenase activity. HupR1 is probably phosphorylated by the sensory component and then acts in conjunction with sigma-54 as a transcriptional activator.

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

Hydrogen uptake protein regulator (HupR) is a member of the nitrogen regulatory protein C (NtrC) family of response regulators. These proteins activate transcription by RNA polymerase (RNAP) in response to a change in environment. This change is detected through the phosphorylation of their receiver domain as part of a two-component signalling pathway. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Also, HupR activates transcription through the more general sigma(70) transcription initiation factor, which does not require activation by ATPase, in contrast to other NtrC family members that utilise sigma(54). Hence, its mode of action is expected to be different from those of the more conventional NtrC family members. We have determined the structures of the unphosphorylated N-terminal receiver domain of wild-type HupR, the mutant HupR(D55E)(N) (which cannot be phosphorylated and down-regulated), and HupR in the presence of the phosphorylation mimic BeF(3)(-). The structures show a typical response regulator fold organised as a dimer whose interface involves alpha4-beta5-alpha5 elements. The interactions across the interface are slightly different between apo and phospho mimics, and these reflect a rearrangement of key conserved residues around the active site aspartate that have been implicated in domain activation in other receiver domain proteins. We also show that the wild-type HupR receiver domain forms a weak dimer in solution, which is strengthened in the presence of the phosphorylation mimic BeF(3)(-). The results indicate many features similar to those that have been observed in other systems, including NtrC (where phosphorylation is activatory), and indicate that recognition properties, which allow HupR to be active in the absence of phosphorylation, lie in the transmission of phosphorylation signals through the linker region to the other domains of the protein.

The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states.,Davies KM, Lowe ED, Venien-Bryan C, Johnson LN J Mol Biol. 2009 Jan 9;385(1):51-64. Epub 2008 Oct 19. PMID:18977359^[1]

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

References

↑ Davies KM, Lowe ED, Venien-Bryan C, Johnson LN. The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states. J Mol Biol. 2009 Jan 9;385(1):51-64. Epub 2008 Oct 19. PMID:18977359 doi:10.1016/j.jmb.2008.10.027

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/2vuh"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE D55E MUTANT OF THE HUPR RECEIVER DOMAIN==
 <StructureSection load='2vuh' size='340' side='right' caption='[[2vuh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vuh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VUH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vuh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VUH FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jk1|2jk1]], [[2vui|2vui]]</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=2vuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vuh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vuh RCSB], [http://www.ebi.ac.uk/pdbsum/2vuh PDBsum]</span></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=2vuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vuh OCA], [http://pdbe.org/2vuh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vuh RCSB], [http://www.ebi.ac.uk/pdbsum/2vuh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vuh ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <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].
+</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=2vuh ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2vuh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rhodobacter capsulatus]]
+[[Category: Rhodonostoc capsulatum molisch 1907]]
 [[Category: Davies, K M]]
 [[Category: Johnson, L N]]

2vuh

From Proteopedia

Revision as of 14:21, 5 August 2016

CRYSTAL STRUCTURE OF THE D55E MUTANT OF THE HUPR RECEIVER DOMAIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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