1q27
From Proteopedia
(New page: 200px<br /><applet load="1q27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q27" /> '''NMR Solution Structure of DR0079: An hypothe...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1q27.gif|left|200px]]<br /><applet load="1q27" size=" | + | [[Image:1q27.gif|left|200px]]<br /><applet load="1q27" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q27" /> | caption="1q27" /> | ||
'''NMR Solution Structure of DR0079: An hypothetical Nudix protein from D. radiodurans'''<br /> | '''NMR Solution Structure of DR0079: An hypothetical Nudix protein from D. radiodurans'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Using nuclear magnetic resonance (NMR) based methods, including residual | + | Using nuclear magnetic resonance (NMR) based methods, including residual dipolar coupling restraints, we have determined the solution structure of the hypothetical Deinococcus radiodurans Nudix protein DR0079 (171 residues, MW = 19.3 kDa). The protein contains eight beta-strands and three alpha-helices organized into three subdomains: an N-terminal beta-sheet (1-34), a central Nudix core (35-140), and a C-terminal helix-turn-helix (141-171). The Nudix core and the C-terminal helix-turn-helix form the fundamental fold common to the Nudix family, a large mixed beta-sheet sandwiched between alpha-helices. The residues that compose the signature Nudix sequence, GX5EX7REUXEEXGU (where U = I, L, or V and X = any amino acid), are contained in a turn-helix-turn motif on the face of the mixed beta-sheet. Chemical shift mapping experiments suggest that DR0079 binds Mg2+. Experiments designed to determine the biological function of the protein indicate that it is not a type I isopentenyl-diphosphate delta-isomerase and that it does not bind alpha,beta-methyleneadenosine 5'-triphosphate (AMPCPP) or guanosine 5'-[beta,gamma-imido]triphosphate (GMPPNP). In this article, the structure of DR0079 is compared to other known Nudix protein structures, a potential substrate-binding surface is proposed, and its possible biological function is discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1Q27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http:// | + | 1Q27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q27 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Buchko, G | + | [[Category: Buchko, G W.]] |
| - | [[Category: Holbrook, S | + | [[Category: Holbrook, S R.]] |
| - | [[Category: Kennedy, M | + | [[Category: Kennedy, M A.]] |
[[Category: Ni, S.]] | [[Category: Ni, S.]] | ||
[[Category: nudix hydrolase]] | [[Category: nudix hydrolase]] | ||
[[Category: radiation resistance]] | [[Category: radiation resistance]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:05 2008'' |
Revision as of 12:35, 21 February 2008
|
NMR Solution Structure of DR0079: An hypothetical Nudix protein from D. radiodurans
Overview
Using nuclear magnetic resonance (NMR) based methods, including residual dipolar coupling restraints, we have determined the solution structure of the hypothetical Deinococcus radiodurans Nudix protein DR0079 (171 residues, MW = 19.3 kDa). The protein contains eight beta-strands and three alpha-helices organized into three subdomains: an N-terminal beta-sheet (1-34), a central Nudix core (35-140), and a C-terminal helix-turn-helix (141-171). The Nudix core and the C-terminal helix-turn-helix form the fundamental fold common to the Nudix family, a large mixed beta-sheet sandwiched between alpha-helices. The residues that compose the signature Nudix sequence, GX5EX7REUXEEXGU (where U = I, L, or V and X = any amino acid), are contained in a turn-helix-turn motif on the face of the mixed beta-sheet. Chemical shift mapping experiments suggest that DR0079 binds Mg2+. Experiments designed to determine the biological function of the protein indicate that it is not a type I isopentenyl-diphosphate delta-isomerase and that it does not bind alpha,beta-methyleneadenosine 5'-triphosphate (AMPCPP) or guanosine 5'-[beta,gamma-imido]triphosphate (GMPPNP). In this article, the structure of DR0079 is compared to other known Nudix protein structures, a potential substrate-binding surface is proposed, and its possible biological function is discussed.
About this Structure
1Q27 is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
Solution structure of hypothetical Nudix hydrolase DR0079 from extremely radiation-resistant Deinococcus radiodurans bacterium., Buchko GW, Ni S, Holbrook SR, Kennedy MA, Proteins. 2004 Jul 1;56(1):28-39. PMID:15162484
Page seeded by OCA on Thu Feb 21 14:35:05 2008
