1n13: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /><applet load="1n13" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n13, resolution 1.40Å" /> '''The Crystal Structur... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1n13.gif|left|200px]]<br /><applet load="1n13" size=" | [[Image:1n13.gif|left|200px]]<br /><applet load="1n13" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1n13, resolution 1.40Å" /> | caption="1n13, resolution 1.40Å" /> | ||
'''The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii'''<br /> | '''The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii'''<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== | ||
1N13 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 and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | 1N13 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> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1N13 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[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: MRD]] | [[Category: MRD]] | ||
| Line 26: | Line 26: | ||
[[Category: pyruvoyl group]] | [[Category: pyruvoyl group]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:05 2008'' | ||
