1ti7

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[[Image:1ti7.jpg|left|200px]]<br /><applet load="1ti7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ti7.jpg|left|200px]]
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caption="1ti7, resolution 1.70&Aring;" />
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'''CRYSTAL STRUCTURE OF NMRA, A NEGATIVE TRANSCRIPTIONAL REGULATOR, IN COMPLEX WITH NADP AT 1.7A RESOLUTION'''<br />
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{{Structure
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|PDB= 1ti7 |SIZE=350|CAPTION= <scene name='initialview01'>1ti7</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE= NMRA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162425 Emericella nidulans])
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}}
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'''CRYSTAL STRUCTURE OF NMRA, A NEGATIVE TRANSCRIPTIONAL REGULATOR, IN COMPLEX WITH NADP AT 1.7A RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1TI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1PDS. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI7 OCA].
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1TI7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]. This structure supersedes the now removed PDB entry 1PDS. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI7 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12764138 12764138]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12764138 12764138]
[[Category: Emericella nidulans]]
[[Category: Emericella nidulans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transcriptional regulation]]
[[Category: transcriptional regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:18:41 2008''

Revision as of 12:18, 20 March 2008

Image:1ti7.jpg


PDB ID 1ti7

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: , , and
Gene: NMRA (Emericella nidulans)
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF NMRA, A NEGATIVE TRANSCRIPTIONAL REGULATOR, IN COMPLEX WITH NADP AT 1.7A RESOLUTION


Overview

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.

About this Structure

1TI7 is a Single protein structure of sequence from Emericella nidulans. This structure supersedes the now removed PDB entry 1PDS. Full crystallographic information is available from OCA.

Reference

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

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