1mt1
From Proteopedia
(New page: 200px<br /><applet load="1mt1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mt1, resolution 2.20Å" /> '''The Crystal Structur...) |
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| - | [[Image:1mt1.gif|left|200px]]<br /><applet load="1mt1" size=" | + | [[Image:1mt1.gif|left|200px]]<br /><applet load="1mt1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mt1, resolution 2.20Å" /> | caption="1mt1, resolution 2.20Å" /> | ||
'''The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannaschii'''<br /> | '''The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannaschii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of pyruvoyl-dependent arginine | + | 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== | ||
| - | 1MT1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with AG2 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:// | + | 1MT1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=AG2:'>AG2</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=1MT1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Ealick, S | + | [[Category: Ealick, S E.]] |
| - | [[Category: Graham, D | + | [[Category: Graham, D E.]] |
| - | [[Category: Tolbert, W | + | [[Category: Tolbert, W D.]] |
| - | [[Category: White, R | + | [[Category: White, R H.]] |
[[Category: AG2]] | [[Category: AG2]] | ||
[[Category: agmatine]] | [[Category: agmatine]] | ||
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[[Category: pyruvoyl group]] | [[Category: pyruvoyl group]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:43 2008'' |
Revision as of 11:58, 21 February 2008
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The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from 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
1MT1 is a Protein complex structure of sequences 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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