1h79
From Proteopedia
(New page: 200px<br /> <applet load="1h79" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h79, resolution 2.9Å" /> '''STRUCTURAL BASIS FOR...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H79 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]] with MG, FE2 and TTP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.2 1.17.4.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H79 OCA]]. | + | 1H79 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]] with MG, FE2 and TTP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.2 1.17.4.2]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H79 OCA]]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:31:30 2007'' |
Revision as of 06:26, 30 October 2007
|
STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DTTP
Overview
BACKGROUND: The specificity of ribonucleotide reductases (RNRs) toward, their four substrates is governed by the binding of deoxyribonucleoside, triphosphates (dNTPs) to the allosteric specificity site. Similar patterns, in the kinetics of allosteric regulation have been a strong argument for a, common evolutionary origin of the three otherwise widely divergent RNR, classes. Recent structural information settled the case for divergent, evolution; however, the structural basis for transmission of the, allosteric signal is currently poorly understood. A comparative study of, the conformational effects of the binding of different effectors has not, yet been possible; in addition, only one RNR class has been studied., RESULTS: Our presentation of the structures of a class III anaerobic RNR, ... [(full description)]
About this Structure
1H79 is a [Single protein] structure of sequence from [Bacteriophage t4] with MG, FE2 and TTP as [ligands]. Active as [Oxidoreductase], with EC number [1.17.4.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases., Larsson KM, Andersson J, Sjoberg BM, Nordlund P, Logan DT, Structure. 2001 Aug;9(8):739-50. PMID:11587648
Page seeded by OCA on Tue Oct 30 08:31:30 2007
