2vbs

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(New page: 200px<br /><applet load="2vbs" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vbs, resolution 3.00&Aring;" /> '''RIBOFLAVIN KINASE MJ...)
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==Overview==
==Overview==
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Proteins of the cradle-loop barrel metafold are formed by duplication of a, conserved betaalphabeta-element, suggesting a common evolutionary origin, from an ancestral group of nucleic acid-binding proteins. The basal fold, within this metafold, the RIFT barrel, is also found in a wide range of, enzymes, whose homologous relationship with the nucleic acid-binding group, is unclear. We have characterized a protein family that is intermediate in, sequence and structure between the basal group of cradle-loop barrels and, one family of RIFT-barrel enzymes, the riboflavin kinases. We report the, structure, substrate-binding mode, and catalytic activity for one of these, proteins, Methanocaldococcus jannaschii Mj0056, which is an archaeal, riboflavin kinase. Mj0056 is unusual in utilizing CTP rather than ATP as, the donor nucleotide, and sequence conservation in the relevant residues, suggests that this is a general feature of archaeal riboflavin kinases.
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Proteins of the cradle-loop barrel metafold are formed by duplication of a conserved betaalphabeta-element, suggesting a common evolutionary origin from an ancestral group of nucleic acid-binding proteins. The basal fold within this metafold, the RIFT barrel, is also found in a wide range of enzymes, whose homologous relationship with the nucleic acid-binding group is unclear. We have characterized a protein family that is intermediate in sequence and structure between the basal group of cradle-loop barrels and one family of RIFT-barrel enzymes, the riboflavin kinases. We report the structure, substrate-binding mode, and catalytic activity for one of these proteins, Methanocaldococcus jannaschii Mj0056, which is an archaeal riboflavin kinase. Mj0056 is unusual in utilizing CTP rather than ATP as the donor nucleotide, and sequence conservation in the relevant residues suggests that this is a general feature of archaeal riboflavin kinases.
==About this Structure==
==About this Structure==
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2VBS 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>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Po4 Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Cl Binding Site For Chain A'>AC3</scene> and <scene name='pdbsite=AC4:Cl Binding Site For Chain A'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBS OCA].
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2VBS 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>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene> and <scene name='pdbsite=AC4:Cl+Binding+Site+For+Chain+A'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBS OCA].
==Reference==
==Reference==
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A CTP-Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle-Loop Barrels., Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M, Structure. 2007 Dec;15(12):1577-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18073108 18073108]
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A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels., Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M, Structure. 2007 Dec;15(12):1577-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18073108 18073108]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ammelburg, M.]]
[[Category: Ammelburg, M.]]
[[Category: Djuranovic, S.]]
[[Category: Djuranovic, S.]]
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[[Category: Hartmann, M.D.]]
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[[Category: Hartmann, M D.]]
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[[Category: Lupas, A.N.]]
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[[Category: Lupas, A N.]]
[[Category: Martin, J.]]
[[Category: Martin, J.]]
[[Category: Zeth, K.]]
[[Category: Zeth, K.]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:24:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:52 2008''

Revision as of 16:54, 21 February 2008


2vbs, resolution 3.00Å

Drag the structure with the mouse to rotate

RIBOFLAVIN KINASE MJ0056 FROM METHANOCALDOCOCCUS JANNASCHII IN COMPLEX WITH PO4

Overview

Proteins of the cradle-loop barrel metafold are formed by duplication of a conserved betaalphabeta-element, suggesting a common evolutionary origin from an ancestral group of nucleic acid-binding proteins. The basal fold within this metafold, the RIFT barrel, is also found in a wide range of enzymes, whose homologous relationship with the nucleic acid-binding group is unclear. We have characterized a protein family that is intermediate in sequence and structure between the basal group of cradle-loop barrels and one family of RIFT-barrel enzymes, the riboflavin kinases. We report the structure, substrate-binding mode, and catalytic activity for one of these proteins, Methanocaldococcus jannaschii Mj0056, which is an archaeal riboflavin kinase. Mj0056 is unusual in utilizing CTP rather than ATP as the donor nucleotide, and sequence conservation in the relevant residues suggests that this is a general feature of archaeal riboflavin kinases.

About this Structure

2VBS is a Single protein structure of sequence from Methanocaldococcus jannaschii with , and as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

Reference

A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels., Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M, Structure. 2007 Dec;15(12):1577-90. PMID:18073108

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