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- | [[Image:1k6i.gif|left|200px]] | |
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- | {{Structure
| + | ==Crystal structure of Nmra, a negative transcriptional regulator (Trigonal form)== |
- | |PDB= 1k6i |SIZE=350|CAPTION= <scene name='initialview01'>1k6i</scene>, resolution 1.80Å
| + | <StructureSection load='1k6i' size='340' side='right'caption='[[1k6i]], [[Resolution|resolution]] 1.80Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
| + | <table><tr><td colspan='2'>[[1k6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K6I FirstGlance]. <br> |
- | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
- | |GENE= nmrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162425 Emericella nidulans])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
- | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6i OCA], [https://pdbe.org/1k6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k6i RCSB], [https://www.ebi.ac.uk/pdbsum/1k6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k6i ProSAT]</span></td></tr> |
- | |RELATEDENTRY= | + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6i OCA], [http://www.ebi.ac.uk/pdbsum/1k6i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k6i RCSB]</span>
| + | == Function == |
- | }}
| + | [https://www.uniprot.org/uniprot/NMRA_EMENI NMRA_EMENI] May be a redox sensor protein. Has much higher affinity for NAD(P) than for NAD(P)H. Has similar affinity for NAD and NADP. Negative transcriptional regulator involved in the post-transcriptional modulation of the GATA-type transcription factor areA, forming part of a system controlling nitrogen metabolite repression (By similarity). Interferes with the interaction between areA and target DNA. Overexpression leads to areA inhibition.<ref>PMID:17854403</ref> <ref>PMID:12764138</ref> <ref>PMID:15537757</ref> <ref>PMID:18602114</ref> |
- | | + | == Evolutionary Conservation == |
- | '''Crystal structure of Nmra, a negative transcriptional regulator (Trigonal form)'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
- | | + | Check<jmol> |
- | | + | <jmolCheckbox> |
- | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/1k6i_consurf.spt"</scriptWhenChecked> |
- | NmrA is a negative transcriptional regulator involved in the post-translational modulation of the GATA-type transcription factor AreA, forming part of a system controlling nitrogen metabolite repression in various fungi. X-ray structures of two NmrA crystal forms, both to 1.8 A resolution, show NmrA consists of two domains, including a Rossmann fold. NmrA shows an unexpected similarity to the short-chain dehydrogenase/reductase (SDR) family, with the closest relationship to UDP-galactose 4-epimerase. We show that NAD binds to NmrA, a previously unreported nucleotide binding property for this protein. NmrA is unlikely to be an active dehydrogenase, however, as the conserved catalytic tyrosine in SDRs is absent in NmrA, and thus the nucleotide binding to NmrA could have a regulatory function. Our results suggest that other transcription factors possess the SDR fold with functions including RNA binding. The SDR fold appears to have been adapted for other roles including non-enzymatic control functions such as transcriptional regulation and is likely to be more widespread than previously recognized.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
- | | + | <text>to colour the structure by Evolutionary Conservation</text> |
- | ==About this Structure== | + | </jmolCheckbox> |
- | 1K6I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6I OCA].
| + | </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=1k6i ConSurf]. |
- | | + | <div style="clear:both"></div> |
- | ==Reference== | + | == References == |
- | The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases., Stammers DK, Ren J, Leslie K, Nichols CE, Lamb HK, Cocklin S, Dodds A, Hawkins AR, EMBO J. 2001 Dec 3;20(23):6619-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11726498 11726498]
| + | <references/> |
- | [[Category: Emericella nidulans]] | + | __TOC__ |
- | [[Category: Single protein]] | + | </StructureSection> |
- | [[Category: Cocklin, S.]] | + | [[Category: Aspergillus nidulans]] |
- | [[Category: Dodds, A.]] | + | [[Category: Large Structures]] |
- | [[Category: Hawkins, A R.]] | + | [[Category: Cocklin S]] |
- | [[Category: Lamb, H K.]] | + | [[Category: Dodds A]] |
- | [[Category: Leslie, K.]] | + | [[Category: Hawkins AR]] |
- | [[Category: Nichols, C E.]] | + | [[Category: Lamb HK]] |
- | [[Category: Ren, J.]] | + | [[Category: Leslie K]] |
- | [[Category: Stammers, D K.]] | + | [[Category: Nichols CE]] |
- | [[Category: rossmann fold transcriptional regulation short chain dehydrogenase reductase]]
| + | [[Category: Ren J]] |
- | | + | [[Category: Stammers DK]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:05 2008''
| + | |
| Structural highlights
Function
NMRA_EMENI May be a redox sensor protein. Has much higher affinity for NAD(P) than for NAD(P)H. Has similar affinity for NAD and NADP. Negative transcriptional regulator involved in the post-transcriptional modulation of the GATA-type transcription factor areA, forming part of a system controlling nitrogen metabolite repression (By similarity). Interferes with the interaction between areA and target DNA. Overexpression leads to areA inhibition.[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.
References
- ↑ Wong KH, Hynes MJ, Todd RB, Davis MA. Transcriptional control of nmrA by the bZIP transcription factor MeaB reveals a new level of nitrogen regulation in Aspergillus nidulans. Mol Microbiol. 2007 Oct;66(2):534-51. Epub 2007 Sep 10. PMID:17854403 doi:http://dx.doi.org/10.1111/j.1365-2958.2007.05940.x
- ↑ Lamb HK, Leslie K, Dodds AL, Nutley M, Cooper A, Johnson C, Thompson P, Stammers DK, Hawkins AR. The negative transcriptional regulator NmrA discriminates between oxidized and reduced dinucleotides. J Biol Chem. 2003 Aug 22;278(34):32107-14. Epub 2003 May 22. PMID:12764138 doi:10.1074/jbc.M304104200
- ↑ Lamb HK, Ren J, Park A, Johnson C, Leslie K, Cocklin S, Thompson P, Mee C, Cooper A, Stammers DK, Hawkins AR. Modulation of the ligand binding properties of the transcription repressor NmrA by GATA-containing DNA and site-directed mutagenesis. Protein Sci. 2004 Dec;13(12):3127-38. Epub 2004 Nov 10. PMID:15537757 doi:10.1110/ps.04958904
- ↑ Kotaka M, Johnson C, Lamb HK, Hawkins AR, Ren J, Stammers DK. Structural analysis of the recognition of the negative regulator NmrA and DNA by the zinc finger from the GATA-type transcription factor AreA. J Mol Biol. 2008 Aug 29;381(2):373-82. Epub 2008 Jun 5. PMID:18602114 doi:http://dx.doi.org/10.1016/j.jmb.2008.05.077
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