|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2wv0' size='340' side='right'caption='[[2wv0]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2wv0' size='340' side='right'caption='[[2wv0]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wv0]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WV0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WV0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wv0]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WV0 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wv0 OCA], [http://pdbe.org/2wv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wv0 RCSB], [http://www.ebi.ac.uk/pdbsum/2wv0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wv0 ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wv0 OCA], [https://pdbe.org/2wv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wv0 RCSB], [https://www.ebi.ac.uk/pdbsum/2wv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wv0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YVOA_BACSU YVOA_BACSU]] Acts as a weak repressor of yflG expression. | + | [https://www.uniprot.org/uniprot/NAGR_BACSU NAGR_BACSU] Main transcriptional repressor of genes involved in N-acetylglucosamine (GlcNAc) transport and utilization (PubMed:21602348, PubMed:20047956, PubMed:24673833). Represses the expression of the nagAB and nagP operons by binding directly within their upstream regions (PubMed:21602348, PubMed:24673833). Binds to the DNA consensus sequence 5'-ATTGGTATAGACAACT-3' (PubMed:21602348). Also acts as a weak repressor of mapB expression (PubMed:16207374).<ref>PMID:16207374</ref> <ref>PMID:20047956</ref> <ref>PMID:21602348</ref> <ref>PMID:24673833</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 35: |
| | [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Muller, Y A]] | + | [[Category: Muller YA]] |
| - | [[Category: Resch, M]] | + | [[Category: Resch M]] |
| - | [[Category: Schiltz, E]] | + | [[Category: Schiltz E]] |
| - | [[Category: Titgemeyer, F]] | + | [[Category: Titgemeyer F]] |
| - | [[Category: Chorismate lyase fold]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Gntr/hutc family]]
| + | |
| - | [[Category: Repressor]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Transcriptional regulator]]
| + | |
| Structural highlights
Function
NAGR_BACSU Main transcriptional repressor of genes involved in N-acetylglucosamine (GlcNAc) transport and utilization (PubMed:21602348, PubMed:20047956, PubMed:24673833). Represses the expression of the nagAB and nagP operons by binding directly within their upstream regions (PubMed:21602348, PubMed:24673833). Binds to the DNA consensus sequence 5'-ATTGGTATAGACAACT-3' (PubMed:21602348). Also acts as a weak repressor of mapB expression (PubMed:16207374).[1] [2] [3] [4]
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
YvoA is a GntR/HutC transcription regulator from Bacillus subtilis implicated in the regulation of genes from the N-acetylglucosamine-degrading pathway. Its 2.4-A crystal structure reveals a homodimeric assembly with each monomer displaying a two-domain fold. The C-terminal domain, which binds the effector N-acetylglucosamine-6-phosphate, adopts a chorismate lyase fold, whereas the N-terminal domain contains a winged helix-turn-helix DNA-binding domain. Isothermal titration calorimetry and site-directed mutagenesis revealed that the effector-binding site in YvoA coincides with the active site of related chorismate lyase from Escherichia coli. The characterization of the DNA- and effector-binding properties of two disulfide-bridged mutants that lock YvoA in two distinct conformational states provides for the first time detailed insight into the allosteric mechanism through which effector binding modulates DNA binding and, thereby regulates transcription in a representative GntR/HutC family member. Central to this allosteric coupling mechanism is a loop-to-helix transition with the dipole of the newly formed helix pointing toward the phosphate of the effector. This transition goes in hand with the emergence of internal symmetry in the effector-binding domain and, in addition, leads to a 122 degrees rotation of the DNA-binding domains that is best described as a jumping-jack-like motion.
Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA.,Resch M, Schiltz E, Titgemeyer F, Muller YA Nucleic Acids Res. 2010 Apr;38(7):2485-97. Epub 2010 Jan 4. PMID:20047956[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ You C, Lu H, Sekowska A, Fang G, Wang Y, Gilles AM, Danchin A. The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis. BMC Microbiol. 2005 Oct 5;5:57. PMID:16207374 doi:10.1186/1471-2180-5-57
- ↑ Resch M, Schiltz E, Titgemeyer F, Muller YA. Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA. Nucleic Acids Res. 2010 Apr;38(7):2485-97. Epub 2010 Jan 4. PMID:20047956 doi:10.1093/nar/gkp1191
- ↑ Bertram R, Rigali S, Wood N, Lulko AT, Kuipers OP, Titgemeyer F. Regulon of the N-acetylglucosamine utilization regulator NagR in Bacillus subtilis. J Bacteriol. 2011 Jul;193(14):3525-36. PMID:21602348 doi:10.1128/JB.00264-11
- ↑ Gaugué I, Oberto J, Plumbridge J. Regulation of amino sugar utilization in Bacillus subtilis by the GntR family regulators, NagR and GamR. Mol Microbiol. 2014 Apr;92(1):100-15. PMID:24673833 doi:10.1111/mmi.12544
- ↑ Resch M, Schiltz E, Titgemeyer F, Muller YA. Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA. Nucleic Acids Res. 2010 Apr;38(7):2485-97. Epub 2010 Jan 4. PMID:20047956 doi:10.1093/nar/gkp1191
|
