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.


1xjm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xjm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xjm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xjm| PDB=1xjm | SCENE= }}
{{STRUCTURE_1xjm| PDB=1xjm | SCENE= }}
-
'''Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dTTP complex'''
+
===Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dTTP complex===
-
==Overview==
+
<!--
-
Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides into deoxyribonucleotides, which constitute the precursor pools used for DNA synthesis and repair. Imbalances in these pools increase mutational rates and are detrimental to the cell. Balanced precursor pools are maintained primarily through the regulation of the RNR substrate specificity. Here, the molecular mechanism of the allosteric substrate specificity regulation is revealed through the structures of a dimeric coenzyme B12-dependent RNR from Thermotoga maritima, both in complexes with four effector-substrate nucleotide pairs and in three complexes with only effector. The mechanism is based on the flexibility of loop 2, a key structural element, which forms a bridge between the specificity effector and substrate nucleotides. Substrate specificity is achieved as different effectors and their cognate substrates stabilize specific discrete loop 2 conformations. The mechanism of substrate specificity regulation is probably general for most class I and class II RNRs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15475969}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15475969 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15475969}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Ribonucleotide reductase]]
[[Category: Ribonucleotide reductase]]
[[Category: Substrate specificity]]
[[Category: Substrate specificity]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:06:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:16:48 2008''

Revision as of 22:16, 27 July 2008

Image:1xjm.png

Template:STRUCTURE 1xjm

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dTTP complex

Template:ABSTRACT PUBMED 15475969

About this Structure

1XJM is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase., Larsson KM, Jordan A, Eliasson R, Reichard P, Logan DT, Nordlund P, Nat Struct Mol Biol. 2004 Nov;11(11):1142-9. Epub 2004 Oct 10. PMID:15475969

Page seeded by OCA on Mon Jul 28 01:16:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xjm"
Personal tools