1n13: Difference between revisions

Revision as of 04:19, 28 July 2008

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File:1n13.png

Template:STRUCTURE 1n13

The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashiiThe Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii

Template:ABSTRACT PUBMED 12623016

About this StructureAbout this Structure

1N13 is a Protein complex structure of sequences from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii'''
+===The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12623016}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12623016}}
 ==About this Structure==
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 [[Category: Pyruvate]]
 [[Category: Pyruvoyl group]]
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