This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1q27

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q27.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1q27.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q27| PDB=1q27 | SCENE= }}
{{STRUCTURE_1q27| PDB=1q27 | SCENE= }}
-
'''NMR Solution Structure of DR0079: An hypothetical Nudix protein from D. radiodurans'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15162484}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15162484 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15162484}}
==About this Structure==
==About this Structure==
-
1Q27 is a [[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].
+
1Q27 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q27 OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Nudix hydrolase]]
[[Category: Nudix hydrolase]]
[[Category: Radiation resistance]]
[[Category: Radiation resistance]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:46:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:51:49 2008''

Revision as of 12:51, 27 July 2008

Template:STRUCTURE 1q27

NMR Solution Structure of DR0079: An hypothetical Nudix protein from D. radiodurans

Template:ABSTRACT PUBMED 15162484

About this Structure

1Q27 is a Single protein structure of sequence from Deinococcus radiodurans. Full experimental 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 Sun Jul 27 15:51:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools