2aya
From Proteopedia
(New page: 200px<br /><applet load="2aya" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aya" /> '''Solution Structure of the C-Terminal 14 kDa ...) |
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'''Solution Structure of the C-Terminal 14 kDa Domain of the tau subunit from Escherichia coli DNA Polymerase III'''<br /> | '''Solution Structure of the C-Terminal 14 kDa Domain of the tau subunit from Escherichia coli DNA Polymerase III'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http:// | + | 2AYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: kh-fold]] | [[Category: kh-fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:05:56 2008'' |
Revision as of 12:05, 23 January 2008
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Solution Structure of the C-Terminal 14 kDa Domain of the tau subunit from Escherichia coli DNA Polymerase III
Overview
The solution structure of the C-terminal Domain V of the tau subunit of E., coli DNA polymerase III was determined by nuclear magnetic resonance (NMR), spectroscopy. The fold is unique to tau subunits. Amino acid sequence, conservation is pronounced for hydrophobic residues that form the, structural core of the protein, indicating that the fold is representative, for tau subunits from a wide range of different bacteria. The interaction, between the polymerase subunits tau and alpha was studied by NMR, experiments where alpha was incubated with full-length C-terminal domain, (tau(C)16), and domains shortened at the C-terminus by 11 and 18 residues, respectively. The only interacting residues were found in the C-terminal, 30-residue segment of tau, most of which is structurally disordered in, free tau(C)16. Since the N- and C-termini of the structured core of, tau(C)16 are located close to each other, this limits the possible, distance between alpha and the pentameric deltatau2gammadelta', clamp-loader complex and, hence, between the two alpha subunits involved, in leading- and lagging-strand DNA synthesis. Analysis of an N-terminally, extended construct (tau(C)22) showed that tau(C)14 presents the only part, of Domains IVa and V of tau which comprises a globular fold in the absence, of other interaction partners.
About this Structure
2AYA is a Single protein structure of sequence from Escherichia coli. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Solution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit., Su XC, Jergic S, Keniry MA, Dixon NE, Otting G, Nucleic Acids Res. 2007;35(9):2825-32. Epub 2007 Apr 22. PMID:17452361
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