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| | ==Solid-State MAS NMR structure of the dimer Crh== | | ==Solid-State MAS NMR structure of the dimer Crh== |
| - | <StructureSection load='2rlz' size='340' side='right'caption='[[2rlz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2rlz' size='340' side='right'caption='[[2rlz]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2rlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLZ FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2rlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLZ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crh, yvcM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=2rlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rlz OCA], [https://pdbe.org/2rlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rlz RCSB], [https://www.ebi.ac.uk/pdbsum/2rlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rlz 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=2rlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rlz OCA], [https://pdbe.org/2rlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rlz RCSB], [https://www.ebi.ac.uk/pdbsum/2rlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rlz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baldus, M]] | + | [[Category: Baldus M]] |
| - | [[Category: Bardiaux, B]] | + | [[Category: Bardiaux B]] |
| - | [[Category: Blanchet, C]] | + | [[Category: Blanchet C]] |
| - | [[Category: Bockmann, A]] | + | [[Category: Bockmann A]] |
| - | [[Category: Gardiennet, C]] | + | [[Category: Gardiennet C]] |
| - | [[Category: Loquet, A]] | + | [[Category: Loquet A]] |
| - | [[Category: Malliavin, T]] | + | [[Category: Malliavin T]] |
| - | [[Category: Nilges, M]] | + | [[Category: Nilges M]] |
| - | [[Category: Dimer]]
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| - | [[Category: Domain-swap]]
| + | |
| - | [[Category: Ma]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
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
In a wide variety of proteins, insolubility presents a challenge to structural biology, as X-ray crystallography and liquid-state NMR are unsuitable. Indeed, no general approach is available as of today for studying the three-dimensional structures of membrane proteins and protein fibrils. We here demonstrate, at the example of the microcrystalline model protein Crh, how high-resolution 3D structures can be derived from magic-angle spinning solid-state NMR distance restraints for fully labeled protein samples. First, we show that proton-mediated rare-spin correlation spectra, as well as carbon-13 spin diffusion experiments, provide enough short, medium, and long-range structural restraints to obtain high-resolution structures of this 2 x 10.4 kDa dimeric protein. Nevertheless, the large number of 13C/15N spins present in this protein, combined with solid-state NMR line widths of about 0.5-1 ppm, induces substantial ambiguities in resonance assignments, preventing 3D structure determination by using distance restraints uniquely assigned on the basis of their chemical shifts. In the second part, we thus demonstrate that an automated iterative assignment algorithm implemented in a dedicated solid-state NMR version of the program ARIA permits to resolve the majority of ambiguities and to calculate a de novo 3D structure from highly ambiguous solid-state NMR data, using a unique fully labeled protein sample. We present, using distance restraints obtained through the iterative assignment process, as well as dihedral angle restraints predicted from chemical shifts, the 3D structure of the fully labeled Crh dimer refined at a root-mean-square deviation of 1.33 A.
3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints.,Loquet A, Bardiaux B, Gardiennet C, Blanchet C, Baldus M, Nilges M, Malliavin T, Bockmann A J Am Chem Soc. 2008 Mar 19;130(11):3579-89. Epub 2008 Feb 20. PMID:18284240[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
- ↑ Loquet A, Bardiaux B, Gardiennet C, Blanchet C, Baldus M, Nilges M, Malliavin T, Bockmann A. 3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints. J Am Chem Soc. 2008 Mar 19;130(11):3579-89. Epub 2008 Feb 20. PMID:18284240 doi:10.1021/ja078014t
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