1n2m

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(New page: 200px<br /><applet load="1n2m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n2m, resolution 1.90&Aring;" /> '''The S53A Proenzyme S...)
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[[Image:1n2m.jpg|left|200px]]<br /><applet load="1n2m" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n2m, resolution 1.90&Aring;" />
caption="1n2m, resolution 1.90&Aring;" />
'''The S53A Proenzyme Structure of Methanococcus jannaschii.'''<br />
'''The S53A Proenzyme Structure of Methanococcus jannaschii.'''<br />
==Overview==
==Overview==
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The three-dimensional structure of pyruvoyl-dependent arginine, decarboxylase from Methanococcus jannaschii was determined at 1.4 A, resolution. The pyruvoyl group of arginine decarboxylase is generated by, an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme, resulting in two polypeptide chains. The structure of the nonprocessing, S53A mutant was also determined. The active site of the processed enzyme, unexpectedly contained the reaction product agmatine. The crystal, structure confirms that arginine decarboxylase is a homotrimer. The, protomer fold is a four-layer alphabetabetaalpha sandwich with topology, similar to pyruvoyl-dependent histidine decarboxylase. Highly conserved, residues Asn47, Ser52, Ser53, Ile54, and Glu109 are proposed to play roles, in the self-processing reaction. Agmatine binding residues include the C, terminus of the beta chain (Ser52) from one protomer and the Asp35 side, chain and the Gly44 and Val46 carbonyl oxygen atoms from an adjacent, protomer. Glu109 is proposed to play a catalytic role in the, decarboxylation reaction.
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The three-dimensional structure of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii was determined at 1.4 A resolution. The pyruvoyl group of arginine decarboxylase is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains. The structure of the nonprocessing S53A mutant was also determined. The active site of the processed enzyme unexpectedly contained the reaction product agmatine. The crystal structure confirms that arginine decarboxylase is a homotrimer. The protomer fold is a four-layer alphabetabetaalpha sandwich with topology similar to pyruvoyl-dependent histidine decarboxylase. Highly conserved residues Asn47, Ser52, Ser53, Ile54, and Glu109 are proposed to play roles in the self-processing reaction. Agmatine binding residues include the C terminus of the beta chain (Ser52) from one protomer and the Asp35 side chain and the Gly44 and Val46 carbonyl oxygen atoms from an adjacent protomer. Glu109 is proposed to play a catalytic role in the decarboxylation reaction.
==About this Structure==
==About this Structure==
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1N2M 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 MRD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arginine_decarboxylase Arginine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.19 4.1.1.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N2M OCA].
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1N2M 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=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arginine_decarboxylase Arginine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.19 4.1.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N2M OCA].
==Reference==
==Reference==
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[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ealick, S.E.]]
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[[Category: Ealick, S E.]]
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[[Category: Graham, D.E.]]
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[[Category: Graham, D E.]]
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[[Category: Tolbert, W.D.]]
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[[Category: Tolbert, W D.]]
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[[Category: White, R.H.]]
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[[Category: White, R H.]]
[[Category: MRD]]
[[Category: MRD]]
[[Category: agmatine]]
[[Category: agmatine]]
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[[Category: pyruvoyl group]]
[[Category: pyruvoyl group]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:53:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:34 2008''

Revision as of 12:01, 21 February 2008


1n2m, resolution 1.90Å

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The S53A Proenzyme Structure of Methanococcus jannaschii.

Overview

The three-dimensional structure of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii was determined at 1.4 A resolution. The pyruvoyl group of arginine decarboxylase is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains. The structure of the nonprocessing S53A mutant was also determined. The active site of the processed enzyme unexpectedly contained the reaction product agmatine. The crystal structure confirms that arginine decarboxylase is a homotrimer. The protomer fold is a four-layer alphabetabetaalpha sandwich with topology similar to pyruvoyl-dependent histidine decarboxylase. Highly conserved residues Asn47, Ser52, Ser53, Ile54, and Glu109 are proposed to play roles in the self-processing reaction. Agmatine binding residues include the C terminus of the beta chain (Ser52) from one protomer and the Asp35 side chain and the Gly44 and Val46 carbonyl oxygen atoms from an adjacent protomer. Glu109 is proposed to play a catalytic role in the decarboxylation reaction.

About this Structure

1N2M is a Single protein structure of sequence from Methanocaldococcus jannaschii with as ligand. Active as Arginine decarboxylase, with EC number 4.1.1.19 Full crystallographic information is available from OCA.

Reference

Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms., Tolbert WD, Graham DE, White RH, Ealick SE, Structure. 2003 Mar;11(3):285-94. PMID:12623016

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