1mu4

From Proteopedia

(Difference between revisions)

Revision as of 09:29, 5 May 2021

CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)

Structural highlights

1mu4 is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1mo1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CRH_BACSU] Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.^[1] ^[2]

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 crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity.

Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr.,Juy M, Penin F, Favier A, Galinier A, Montserret R, Haser R, Deutscher J, Bockmann A J Mol Biol. 2003 Sep 26;332(4):767-76. PMID:12972249^[3]

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

References

↑ Galinier A, Haiech J, Kilhoffer MC, Jaquinod M, Stulke J, Deutscher J, Martin-Verstraete I. The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8439-44. PMID:9237995
↑ Schumacher MA, Seidel G, Hillen W, Brennan RG. Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation. J Biol Chem. 2006 Mar 10;281(10):6793-800. Epub 2005 Nov 29. PMID:16316990 doi:10.1074/jbc.M509977200
↑ Juy M, Penin F, Favier A, Galinier A, Montserret R, Haser R, Deutscher J, Bockmann A. Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr. J Mol Biol. 2003 Sep 26;332(4):767-76. PMID:12972249

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/1mu4"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mu4' size='340' side='right'caption='[[1mu4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mu4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MU4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mu4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MU4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mo1|1mo1]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mo1|1mo1]]</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=1mu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mu4 OCA], [http://pdbe.org/1mu4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mu4 RCSB], [http://www.ebi.ac.uk/pdbsum/1mu4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mu4 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=1mu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mu4 OCA], [https://pdbe.org/1mu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mu4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mu4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CRH_BACSU CRH_BACSU]] Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.<ref>PMID:9237995</ref> <ref>PMID:16316990</ref>
+[[https://www.uniprot.org/uniprot/CRH_BACSU CRH_BACSU]] Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.<ref>PMID:9237995</ref> <ref>PMID:16316990</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1mu4

From Proteopedia

Revision as of 09:29, 5 May 2021

CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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