2nyf
From Proteopedia
(New page: 200px<br /><applet load="2nyf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nyf, resolution 2.50Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Phenylalanine ammonia lyase (PAL) catalyzes the deamination of | + | 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== | ==About this Structure== | ||
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[[Category: Phenylalanine ammonia-lyase]] | [[Category: Phenylalanine ammonia-lyase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bowman, M | + | [[Category: Bowman, M E.]] |
| - | [[Category: Louie, G | + | [[Category: Louie, G V.]] |
| - | [[Category: Moffitt, M | + | [[Category: Moffitt, M C.]] |
| - | [[Category: Moore, B | + | [[Category: Moore, B S.]] |
| - | [[Category: Noel, J | + | [[Category: Noel, J P.]] |
[[Category: Pence, J.]] | [[Category: Pence, J.]] | ||
[[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 Thu Feb 21 18:12:26 2008'' |
Revision as of 16:12, 21 February 2008
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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. Active as Phenylalanine ammonia-lyase, with EC number 4.3.1.5 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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