2nyn: Difference between revisions

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[[Image:2nyn.gif|left|200px]]
[[Image:2nyn.gif|left|200px]]


{{Structure
<!--
|PDB= 2nyn |SIZE=350|CAPTION= <scene name='initialview01'>2nyn</scene>, resolution 1.90&Aring;
The line below this paragraph, containing "STRUCTURE_2nyn", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-5-HYDROXY-4-METHYL-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_ammonia-lyase Histidine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.3 4.3.1.3] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_2nyn| PDB=2nyn  | SCENE= }}  
|RELATEDENTRY=[[2nyf|2nyf]], [[1w27|1w27]], [[1y2m|1y2m]], [[1t6j|1t6j]], [[1gkm|1gkm]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyn OCA], [http://www.ebi.ac.uk/pdbsum/2nyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nyn RCSB]</span>
}}


'''Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis'''
'''Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis'''
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[[Category: Noel, J P.]]
[[Category: Noel, J P.]]
[[Category: Pence, J.]]
[[Category: Pence, J.]]
[[Category: methylidene imidazolone prosthetic group]]
[[Category: Methylidene imidazolone prosthetic group]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:10:18 2008''

Revision as of 10:05, 4 May 2008

File:2nyn.gif

Template:STRUCTURE 2nyn

Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis


OverviewOverview

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 StructureAbout this Structure

2NYN is a Single protein structure of sequence from Anabaena variabilis. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sun May 4 10:05:10 2008

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