1ilo: Difference between revisions
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'''NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.'''<br /> | '''NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.'''<br /> | ||
==Overview== | ==Overview== | ||
As part of a high-throughput, structural proteomic project we have used | As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains a central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other. It has an overall fold superficially similar to that of a glutaredoxin. However, detailed analysis of its three-dimensional structure along with molecular docking simulations of its interaction with T7 DNA polymerase (a thioredoxin-specific substrate) and comparisons with other known members of the thioredoxin/glutaredoxin family of proteins strongly suggest that MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a) values of its active site thiols along with direct measurements of the thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a thioredoxin and exhibits no glutaredoxin activity. We have also identified a group of previously unknown proteins from several other archaebacteria that have significant (34-44%) sequence identity with MtH895. These proteins have unusual active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On the basis of the results presented here, we predict that these small proteins are all members of a new class of truncated thioredoxins. | ||
==About this Structure== | ==About this Structure== | ||
1ILO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Active as [http://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] Full crystallographic information is available from [http:// | 1ILO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Active as [http://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bhattacharyya, S.]] | [[Category: Bhattacharyya, S.]] | ||
[[Category: Habibi-Nazhad, B.]] | [[Category: Habibi-Nazhad, B.]] | ||
[[Category: NESG, Northeast | [[Category: NESG, Northeast Structural Genomics Consortium.]] | ||
[[Category: Slupsky, C | [[Category: Slupsky, C M.]] | ||
[[Category: Sykes, B | [[Category: Sykes, B D.]] | ||
[[Category: Wishart, D | [[Category: Wishart, D S.]] | ||
[[Category: beta-alpha-beta-alpha-beta-beta-alpha motif]] | [[Category: beta-alpha-beta-alpha-beta-beta-alpha motif]] | ||
[[Category: nesg]] | [[Category: nesg]] | ||
| Line 27: | Line 27: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:06 2008'' | ||
Revision as of 11:13, 21 February 2008
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NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.
Overview
As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains a central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other. It has an overall fold superficially similar to that of a glutaredoxin. However, detailed analysis of its three-dimensional structure along with molecular docking simulations of its interaction with T7 DNA polymerase (a thioredoxin-specific substrate) and comparisons with other known members of the thioredoxin/glutaredoxin family of proteins strongly suggest that MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a) values of its active site thiols along with direct measurements of the thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a thioredoxin and exhibits no glutaredoxin activity. We have also identified a group of previously unknown proteins from several other archaebacteria that have significant (34-44%) sequence identity with MtH895. These proteins have unusual active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On the basis of the results presented here, we predict that these small proteins are all members of a new class of truncated thioredoxins.
About this Structure
1ILO is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Active as Phosphoadenylyl-sulfate reductase (thioredoxin), with EC number 1.8.4.8 Full crystallographic information is available from OCA.
Reference
Identification of a novel archaebacterial thioredoxin: determination of function through structure., Bhattacharyya S, Habibi-Nazhad B, Amegbey G, Slupsky CM, Yee A, Arrowsmith C, Wishart DS, Biochemistry. 2002 Apr 16;41(15):4760-70. PMID:11939770
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Methanothermobacter thermautotrophicus
- Phosphoadenylyl-sulfate reductase (thioredoxin)
- Single protein
- Bhattacharyya, S.
- Habibi-Nazhad, B.
- NESG, Northeast Structural Genomics Consortium.
- Slupsky, C M.
- Sykes, B D.
- Wishart, D S.
- Beta-alpha-beta-alpha-beta-beta-alpha motif
- Nesg
- Northeast structural genomics consortium
- Protein structure initiative
- Psi
- Structural genomics
