1s3l

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(New page: 200px<br /><applet load="1s3l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s3l, resolution 2.40&Aring;" /> '''Structural and Funct...)
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caption="1s3l, resolution 2.40&Aring;" />
'''Structural and Functional Characterization of a Novel Archaeal Phosphodiesterase'''<br />
'''Structural and Functional Characterization of a Novel Archaeal Phosphodiesterase'''<br />
==Overview==
==Overview==
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Methanococcus jannaschii MJ0936 is a hypothetical protein of unknown, function with over 50 homologs found in many bacteria and Archaea. To help, define the molecular (biochemical and biophysical) function of MJ0936, we, determined its crystal structure at 2.4-A resolution and performed a, series of biochemical screens for catalytic activity. The overall fold of, this single domain protein consists of a four-layered structure formed by, two beta-sheets flanked by alpha-helices on both sides. The crystal, structure suggested its biochemical function to be a nuclease, phosphatase, or nucleotidase, with a requirement for some metal ions., Crystallization in the presence of Ni(2+) or Mn(2+) produced a protein, containing a binuclear metal center in the putative active site formed by, a cluster of conserved residues. Analysis of MJ0936 against a panel of, general enzymatic assays revealed catalytic activity toward, bis-p-nitrophenyl phosphate, an indicator substrate for phosphodiesterases, and nucleases. Significant activity was also found with two other, phosphodiesterase substrates, thymidine 5'-monophosphate p-nitrophenyl, ester and p-nitrophenylphosphorylcholine, but no activity was found for, cAMP or cGMP. Phosphodiesterase activity of MJ0936 had an absolute, requirement for divalent metal ions with Ni(2+) and Mn(2+) being most, effective. Thus, our structural and enzymatic studies have identified the, biochemical function of MJ0936 as that of a novel phosphodiesterase.
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Methanococcus jannaschii MJ0936 is a hypothetical protein of unknown function with over 50 homologs found in many bacteria and Archaea. To help define the molecular (biochemical and biophysical) function of MJ0936, we determined its crystal structure at 2.4-A resolution and performed a series of biochemical screens for catalytic activity. The overall fold of this single domain protein consists of a four-layered structure formed by two beta-sheets flanked by alpha-helices on both sides. The crystal structure suggested its biochemical function to be a nuclease, phosphatase, or nucleotidase, with a requirement for some metal ions. Crystallization in the presence of Ni(2+) or Mn(2+) produced a protein containing a binuclear metal center in the putative active site formed by a cluster of conserved residues. Analysis of MJ0936 against a panel of general enzymatic assays revealed catalytic activity toward bis-p-nitrophenyl phosphate, an indicator substrate for phosphodiesterases and nucleases. Significant activity was also found with two other phosphodiesterase substrates, thymidine 5'-monophosphate p-nitrophenyl ester and p-nitrophenylphosphorylcholine, but no activity was found for cAMP or cGMP. Phosphodiesterase activity of MJ0936 had an absolute requirement for divalent metal ions with Ni(2+) and Mn(2+) being most effective. Thus, our structural and enzymatic studies have identified the biochemical function of MJ0936 as that of a novel phosphodiesterase.
==About this Structure==
==About this Structure==
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1S3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with PO4 and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S3L OCA].
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1S3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3L OCA].
==Reference==
==Reference==
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[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Busso, D.]]
[[Category: Busso, D.]]
[[Category: Chen, S.]]
[[Category: Chen, S.]]
[[Category: Jancrick, J.]]
[[Category: Jancrick, J.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
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[[Category: Kim, S.H.]]
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[[Category: Kim, S H.]]
[[Category: Kuznetsova, E.]]
[[Category: Kuznetsova, E.]]
[[Category: Proudfoot, M.]]
[[Category: Proudfoot, M.]]
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[[Category: Yakunin, A.F.]]
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[[Category: Yakunin, A F.]]
[[Category: PO4]]
[[Category: PO4]]
[[Category: UNX]]
[[Category: UNX]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:32 2008''

Revision as of 12:57, 21 February 2008


1s3l, resolution 2.40Å

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Structural and Functional Characterization of a Novel Archaeal Phosphodiesterase

Overview

Methanococcus jannaschii MJ0936 is a hypothetical protein of unknown function with over 50 homologs found in many bacteria and Archaea. To help define the molecular (biochemical and biophysical) function of MJ0936, we determined its crystal structure at 2.4-A resolution and performed a series of biochemical screens for catalytic activity. The overall fold of this single domain protein consists of a four-layered structure formed by two beta-sheets flanked by alpha-helices on both sides. The crystal structure suggested its biochemical function to be a nuclease, phosphatase, or nucleotidase, with a requirement for some metal ions. Crystallization in the presence of Ni(2+) or Mn(2+) produced a protein containing a binuclear metal center in the putative active site formed by a cluster of conserved residues. Analysis of MJ0936 against a panel of general enzymatic assays revealed catalytic activity toward bis-p-nitrophenyl phosphate, an indicator substrate for phosphodiesterases and nucleases. Significant activity was also found with two other phosphodiesterase substrates, thymidine 5'-monophosphate p-nitrophenyl ester and p-nitrophenylphosphorylcholine, but no activity was found for cAMP or cGMP. Phosphodiesterase activity of MJ0936 had an absolute requirement for divalent metal ions with Ni(2+) and Mn(2+) being most effective. Thus, our structural and enzymatic studies have identified the biochemical function of MJ0936 as that of a novel phosphodiesterase.

About this Structure

1S3L is a Single protein structure of sequence from Methanocaldococcus jannaschii with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural and functional characterization of a novel phosphodiesterase from Methanococcus jannaschii., Chen S, Yakunin AF, Kuznetsova E, Busso D, Pufan R, Proudfoot M, Kim R, Kim SH, J Biol Chem. 2004 Jul 23;279(30):31854-62. Epub 2004 May 5. PMID:15128743

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