1ti7: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1ti7.jpg|left|200px]]
{{Seed}}
[[Image:1ti7.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ti7|  PDB=1ti7  |  SCENE=  }}  
{{STRUCTURE_1ti7|  PDB=1ti7  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF NMRA, A NEGATIVE TRANSCRIPTIONAL REGULATOR, IN COMPLEX WITH NADP AT 1.7A RESOLUTION'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_12764138}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12764138 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12764138}}


==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/12764138 12764138]
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]
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]
Expression, purification and crystallization of Aspergillus nidulans NmrA, a negative regulatory protein involved in nitrogen-metabolite repression., Nichols CE, Cocklin S, Dodds A, Ren J, Lamb H, Hawkins AR, Stammers DK, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1722-5. Epub 2001, Oct 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11679757 11679757]
[[Category: Emericella nidulans]]
[[Category: Emericella nidulans]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 38: Line 46:
[[Category: Short chain]]
[[Category: Short chain]]
[[Category: Transcriptional regulation]]
[[Category: Transcriptional regulation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:58:42 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:59:24 2008''
Retrieved from "https://proteopedia.org/1ti7"