1mt1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1mt1.gif|left|200px]] | [[Image:1mt1.gif|left|200px]] | ||
'''The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannaschii''' | {{Structure | ||
|PDB= 1mt1 |SIZE=350|CAPTION= <scene name='initialview01'>1mt1</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=AG2:AGMATINE'>AG2</scene> | |||
|ACTIVITY= [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] | |||
|GENE= MJ0316 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]) | |||
}} | |||
'''The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannaschii''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1MT1 is a [ | 1MT1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MT1 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12623016 12623016] | ||
[[Category: Arginine decarboxylase]] | [[Category: Arginine decarboxylase]] | ||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
| Line 24: | Line 33: | ||
[[Category: pyruvoyl group]] | [[Category: pyruvoyl group]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:47:48 2008'' | ||
Revision as of 13:47, 20 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | MJ0316 (Methanocaldococcus jannaschii) | ||||||
| Activity: | Arginine decarboxylase, with EC number 4.1.1.19 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannaschii
OverviewOverview
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 StructureAbout this Structure
1MT1 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
Page seeded by OCA on Thu Mar 20 12:47:48 2008