1w27
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1w27.gif|left|200px]] | + | [[Image:1w27.gif|left|200px]] |
| - | + | ||
| - | '''PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM''' | + | {{Structure |
| + | |PDB= 1w27 |SIZE=350|CAPTION= <scene name='initialview01'>1w27</scene>, resolution 1.70Å | ||
| + | |SITE= <scene name='pdbsite=MI1:Dtt+Binding+Site+For+Chain+B'>MI1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1W27 is a [ | + | 1W27 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Petroselinum_crispum Petroselinum crispum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W27 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase., Ritter H, Schulz GE, Plant Cell. 2004 Dec;16(12):3426-36. Epub 2004 Nov 17. PMID:[http:// | + | Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase., Ritter H, Schulz GE, Plant Cell. 2004 Dec;16(12):3426-36. Epub 2004 Nov 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15548745 15548745] |
[[Category: Petroselinum crispum]] | [[Category: Petroselinum crispum]] | ||
[[Category: Phenylalanine ammonia-lyase]] | [[Category: Phenylalanine ammonia-lyase]] | ||
| Line 21: | Line 30: | ||
[[Category: phenylpropanoid metabolism]] | [[Category: phenylpropanoid metabolism]] | ||
| - | ''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 14:51:03 2008'' |
Revision as of 12:51, 20 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Phenylalanine ammonia-lyase, with EC number 4.3.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM
Overview
Because of its key role in secondary phenylpropanoid metabolism, Phe ammonia-lyase is one of the most extensively studied plant enzymes. To provide a basis for detailed structure-function studies, the enzyme from parsley (Petroselinum crispum) was crystallized, and the structure was elucidated at 1.7-A resolution. It contains the unusual electrophilic 4-methylidene-imidazole-5-one group, which is derived from a tripeptide segment in two autocatalytic dehydration reactions. The enzyme resembles His ammonia-lyase from the general His degradation pathway but contains 207 additional residues, mainly in an N-terminal extension rigidifying a domain interface and in an inserted alpha-helical domain restricting the access to the active center. Presumably, Phe ammonia-lyase developed from His ammonia-lyase when fungi and plants diverged from the other kingdoms. A pathway of the catalyzed reaction is proposed in agreement with established biochemical data. The inactivation of the enzyme by a nucleophile is described in detail.
About this Structure
1W27 is a Single protein structure of sequence from Petroselinum crispum. Full crystallographic information is available from OCA.
Reference
Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase., Ritter H, Schulz GE, Plant Cell. 2004 Dec;16(12):3426-36. Epub 2004 Nov 17. PMID:15548745
Page seeded by OCA on Thu Mar 20 14:51:03 2008
