1eiw

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eiw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eiw OCA], [http://www.ebi.ac.uk/pdbsum/1eiw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eiw RCSB]</span>
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'''Solution structure of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum'''
'''Solution structure of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum'''
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[[Category: Kennedy, M A.]]
[[Category: Kennedy, M A.]]
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[[Category: NESG, Northeast Structural Genomics Consortium.]]
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[[Category: (a/b)5 doubly wound fold]]
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[[Category: Chey-like fold]]
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[[Category: chey-like fold]]
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[[Category: flavodoxin-like fold]]
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[[Category: nesg]]
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[[Category: Northeast structural genomics consortium]]
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[[Category: northeast structural genomics consortium]]
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[[Category: Parallel beta sheet]]
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[[Category: parallel beta sheet]]
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[[Category: Protein structure initiative]]
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[[Category: protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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[[Category: structural genomic]]
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Revision as of 12:09, 2 May 2008

Template:STRUCTURE 1eiw

Solution structure of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum


Overview

The structure of MTH538, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum, has been determined by NMR spectroscopy. MTH538 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized sequences from this organism. MTH538 is a so-called singleton, a sequence not closely related to any other (known) sequences. The structure of MTH538 closely resembles the known structures of receiver domains from two component response regulator systems, such as CheY, and is similar to the structures of flavodoxins and GTP-binding proteins. Tests on MTH538 for characteristic activities of CheY and flavodoxin were negative. MTH538 did not become phosphorylated in the presence of acetyl phosphate and Mg(2+), although it appeared to bind Mg(2+). MTH538 also did not bind flavin mononucleotide (FMN) or coenzyme F(420). Nevertheless, sequence and structure parallels between MTH538/CheY and two families of ATPase/phosphatase proteins suggest that MTH538 may have a role in a phosphorylation-independent two-component response regulator system.

About this Structure

1EIW is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

Structure-based functional classification of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum., Cort JR, Yee A, Edwards AM, Arrowsmith CH, Kennedy MA, J Mol Biol. 2000 Sep 8;302(1):189-203. PMID:10964569 Page seeded by OCA on Fri May 2 15:09:14 2008

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