1dk4

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(New page: 200px<br /><applet load="1dk4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dk4, resolution 2.6&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1dk4.gif|left|200px]]<br /><applet load="1dk4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dk4, resolution 2.6&Aring;" />
caption="1dk4, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE'''<br />
'''CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE'''<br />
==Overview==
==Overview==
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In sequenced genomes, protein coding regions with unassigned function, constitute between 10 and 50% of all open reading frames. Often key, enzymes cannot be identified using sequence homology searches. For, example, despite the fact that methanogens have an apparently functional, gluconeogenesis pathway, standard tools have been unable to identify a, fructose-1,6-bisphosphatase (FBPase) gene in the sequenced Methanoccocus, jannaschii genome. Using a combination of functional and structural tools, we have shown that the protein product of the M. jannaschii gene MJ0109, which had been tentatively annotated as an inositol monophosphatase, (IMPase), has both IMPase and FBPase activities. Moreover, several gene, products annotated as IMPases from different thermophilic organisms also, possess FBPase activity. Thus, we have found the FBPase that was 'missing', in thermophiles and shown that it also functions as an IMPase.
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In sequenced genomes, protein coding regions with unassigned function constitute between 10 and 50% of all open reading frames. Often key enzymes cannot be identified using sequence homology searches. For example, despite the fact that methanogens have an apparently functional gluconeogenesis pathway, standard tools have been unable to identify a fructose-1,6-bisphosphatase (FBPase) gene in the sequenced Methanoccocus jannaschii genome. Using a combination of functional and structural tools, we have shown that the protein product of the M. jannaschii gene MJ0109, which had been tentatively annotated as an inositol monophosphatase (IMPase), has both IMPase and FBPase activities. Moreover, several gene products annotated as IMPases from different thermophilic organisms also possess FBPase activity. Thus, we have found the FBPase that was 'missing' in thermophiles and shown that it also functions as an IMPase.
==About this Structure==
==About this Structure==
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1DK4 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 ZN and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DK4 OCA].
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1DK4 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=ZN:'>ZN</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DK4 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chen, L.]]
[[Category: Chen, L.]]
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[[Category: Johnson, K.A.]]
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[[Category: Johnson, K A.]]
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[[Category: Roberts, M.F.]]
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[[Category: Roberts, M F.]]
[[Category: Stec, B.]]
[[Category: Stec, B.]]
[[Category: Yang, H.]]
[[Category: Yang, H.]]
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[[Category: homodimer]]
[[Category: homodimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:21:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:22 2008''

Revision as of 10:17, 21 February 2008


1dk4, resolution 2.6Å

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CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE

Overview

In sequenced genomes, protein coding regions with unassigned function constitute between 10 and 50% of all open reading frames. Often key enzymes cannot be identified using sequence homology searches. For example, despite the fact that methanogens have an apparently functional gluconeogenesis pathway, standard tools have been unable to identify a fructose-1,6-bisphosphatase (FBPase) gene in the sequenced Methanoccocus jannaschii genome. Using a combination of functional and structural tools, we have shown that the protein product of the M. jannaschii gene MJ0109, which had been tentatively annotated as an inositol monophosphatase (IMPase), has both IMPase and FBPase activities. Moreover, several gene products annotated as IMPases from different thermophilic organisms also possess FBPase activity. Thus, we have found the FBPase that was 'missing' in thermophiles and shown that it also functions as an IMPase.

About this Structure

1DK4 is a Single protein structure of sequence from Methanocaldococcus jannaschii with and as ligands. Active as Inositol-phosphate phosphatase, with EC number 3.1.3.25 Full crystallographic information is available from OCA.

Reference

MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase., Stec B, Yang H, Johnson KA, Chen L, Roberts MF, Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561

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