1b78

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(New page: 200px<br /><applet load="1b78" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b78, resolution 2.20&Aring;" /> '''STRUCTURE-BASED IDEN...)
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'''STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226'''<br />
'''STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226'''<br />
==Overview==
==Overview==
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Almost half of the entire set of predicted genomic products from, Methanococcus jannaschii are classified as functionally unknown, hypothetical proteins. We present a structure-based identification of the, biochemical function of a protein with an as yet unknown function from a, M. jannaschii gene, Mj0226. The crystal structure of Mj0226 protein, determined at 2.2 A resolution reveals that the protein is a homodimer and, each monomer folds into an elongated alpha/beta structure of a new fold, family. Comparisons of Mj0226 protein with protein structures in the, database, however, indicate that one part of the protein is homologous to, some of the nucleotide-binding proteins. Biochemical analysis shows that, Mj0226 protein is a novel nucleotide triphosphatase that can efficiently, hydrolyze nonstandard nucleotides such as XTP to XMP or ITP to IMP, but, not the standard nucleotides, in the presence of Mg2+ or Mn2+ ions.
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Almost half of the entire set of predicted genomic products from Methanococcus jannaschii are classified as functionally unknown hypothetical proteins. We present a structure-based identification of the biochemical function of a protein with an as yet unknown function from a M. jannaschii gene, Mj0226. The crystal structure of Mj0226 protein determined at 2.2 A resolution reveals that the protein is a homodimer and each monomer folds into an elongated alpha/beta structure of a new fold family. Comparisons of Mj0226 protein with protein structures in the database, however, indicate that one part of the protein is homologous to some of the nucleotide-binding proteins. Biochemical analysis shows that Mj0226 protein is a novel nucleotide triphosphatase that can efficiently hydrolyze nonstandard nucleotides such as XTP to XMP or ITP to IMP, but not the standard nucleotides, in the presence of Mg2+ or Mn2+ ions.
==About this Structure==
==About this Structure==
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1B78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B78 OCA].
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1B78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B78 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cho, Y.]]
[[Category: Cho, Y.]]
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[[Category: Chung, J.H.]]
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[[Category: Chung, J H.]]
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[[Category: Han, Y.S.]]
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[[Category: Han, Y S.]]
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[[Category: Hwang, K.Y.]]
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[[Category: Hwang, K Y.]]
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[[Category: Kim, S.H.]]
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[[Category: Kim, S H.]]
[[Category: hyperthermal protein]]
[[Category: hyperthermal protein]]
[[Category: pyrophosphatase]]
[[Category: pyrophosphatase]]
[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:19 2008''

Revision as of 09:52, 21 February 2008


1b78, resolution 2.20Å

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STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226

Overview

Almost half of the entire set of predicted genomic products from Methanococcus jannaschii are classified as functionally unknown hypothetical proteins. We present a structure-based identification of the biochemical function of a protein with an as yet unknown function from a M. jannaschii gene, Mj0226. The crystal structure of Mj0226 protein determined at 2.2 A resolution reveals that the protein is a homodimer and each monomer folds into an elongated alpha/beta structure of a new fold family. Comparisons of Mj0226 protein with protein structures in the database, however, indicate that one part of the protein is homologous to some of the nucleotide-binding proteins. Biochemical analysis shows that Mj0226 protein is a novel nucleotide triphosphatase that can efficiently hydrolyze nonstandard nucleotides such as XTP to XMP or ITP to IMP, but not the standard nucleotides, in the presence of Mg2+ or Mn2+ ions.

About this Structure

1B78 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Structure-based identification of a novel NTPase from Methanococcus jannaschii., Hwang KY, Chung JH, Kim SH, Han YS, Cho Y, Nat Struct Biol. 1999 Jul;6(7):691-6. PMID:10404228

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