2nyf
From Proteopedia
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|PDB= 2nyf |SIZE=350|CAPTION= <scene name='initialview01'>2nyf</scene>, resolution 2.50Å | |PDB= 2nyf |SIZE=350|CAPTION= <scene name='initialview01'>2nyf</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-5-HYDROXY-4-METHYL-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phenylalanine_ammonia-lyase Phenylalanine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.5 4.3.1.5] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_ammonia-lyase Phenylalanine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.5 4.3.1.5] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1w27|1w27]], [[1y2m|1y2m]], [[1t6j|1t6j]], [[1gkm|1gkm]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyf OCA], [http://www.ebi.ac.uk/pdbsum/2nyf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nyf RCSB]</span> | ||
}} | }} | ||
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[[Category: methylidene imidazolone prosthetic group (autocatalytically formed by internal tripeptide segment ala167-ser168-gly169)]] | [[Category: methylidene imidazolone prosthetic group (autocatalytically formed by internal tripeptide segment ala167-ser168-gly169)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:10:12 2008'' |
Revision as of 01:10, 31 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phenylalanine ammonia-lyase, with EC number 4.3.1.5 | ||||||
| Related: | 1w27, 1y2m, 1t6j, 1gkm
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of phenylalanine ammonia-lyase from Nostoc punctiforme
Overview
Phenylalanine ammonia lyase (PAL) catalyzes the deamination of phenylalanine to cinnamate and ammonia. While PALs are common in terrestrial plants where they catalyze the first committed step in the formation of phenylpropanoids, only a few prokaryotic PALs have been identified to date. Here we describe for the first time PALs from cyanobacteria, in particular, Anabaena variabilis ATCC 29413 and Nostoc punctiforme ATCC 29133, identified by screening the genome sequences of these organisms for members of the aromatic amino acid ammonia lyase family. Both PAL genes associate with secondary metabolite biosynthetic gene clusters as observed for other eubacterial PAL genes. In comparison to eukaryotic homologues, the cyanobacterial PALs are 20% smaller in size but share similar substrate selectivity and kinetic activity toward L-phenylalanine over L-tyrosine. Structure elucidation by protein X-ray crystallography confirmed that the two cyanobacterial PALs are similar in tertiary and quatenary structure to plant and yeast PALs as well as the mechanistically related histidine ammonia lyases.
About this Structure
2NYF is a Protein complex structure of sequences from Nostoc punctiforme. Full crystallographic information is available from OCA.
Reference
Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization., Moffitt MC, Louie GV, Bowman ME, Pence J, Noel JP, Moore BS, Biochemistry. 2007 Jan 30;46(4):1004-12. PMID:17240984
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