1ti7: Difference between revisions
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New page: left|200px<br /><applet load="1ti7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ti7, resolution 1.70Å" /> '''CRYSTAL STRUCTURE OF... |
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== | ==CRYSTAL STRUCTURE OF NMRA, A NEGATIVE TRANSCRIPTIONAL REGULATOR, IN COMPLEX WITH NADP AT 1.7A RESOLUTION== | ||
NmrA, a transcription repressor involved in the regulation of nitrogen | <StructureSection load='1ti7' size='340' side='right'caption='[[1ti7]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ti7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pds 1pds]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TI7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=1ti7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ti7 OCA], [https://pdbe.org/1ti7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ti7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ti7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ti7 ProSAT]</span></td></tr> | |||
</table> | |||
== 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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ti/1ti7_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<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/main_output.php?pdb_ID=1ti7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NmrA, a transcription repressor involved in the regulation of nitrogen metabolism in Aspergillus nidulans,is a member of the short-chain dehydrogenase reductase superfamily. Isothermal titration calorimetry and differential scanning calorimetry have been used to show NmrA binds NAD+ and NADP+ with similar affinity (average KD 65 microM) but has a greatly reduced affinity for NADH and NADPH (average KD 6.0 mM). The structure of NmrA in a complex with NADP+ reveals how repositioning a His-37 side chain allows the different conformations of NAD+ and NADP+ to be accommodated. Modeling NAD(P)H into NmrA indicated that steric clashes, attenuation of electrostatic interactions, and loss of aromatic ring stacking can explain the differing affinities of NAD(P)+/NAD(P)H. The ability of NmrA to discriminate between the oxidized and reduced forms of the dinucleotides may be linked to a possible role in redox sensing. Isothermal titration calorimetry demonstrated that NmrA and a C-terminal fragment of the GATA transcription factor AreA interacted with a 1:1 stoichiometry and an apparent KD of 0.26 microM. NmrA was unable to bind the nitrogen metabolite repression signaling molecules ammonium or glutamine. | |||
The negative transcriptional regulator NmrA discriminates between oxidized and reduced dinucleotides.,Lamb HK, Leslie K, Dodds AL, Nutley M, Cooper A, Johnson C, Thompson P, Stammers DK, Hawkins AR J Biol Chem. 2003 Aug 22;278(34):32107-14. Epub 2003 May 22. PMID:12764138<ref>PMID:12764138</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1ti7" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Cooper | <references/> | ||
[[Category: Dodds | __TOC__ | ||
[[Category: Hawkins | </StructureSection> | ||
[[Category: Johnson | [[Category: Aspergillus nidulans]] | ||
[[Category: Lamb | [[Category: Large Structures]] | ||
[[Category: Leslie | [[Category: Cooper A]] | ||
[[Category: Nutley | [[Category: Dodds AL]] | ||
[[Category: Stammers | [[Category: Hawkins AR]] | ||
[[Category: Thompson | [[Category: Johnson C]] | ||
[[Category: Lamb HK]] | |||
[[Category: Leslie K]] | |||
[[Category: Nutley M]] | |||
[[Category: Stammers DK]] | |||
[[Category: Thompson P]] | |||
