1w27
From Proteopedia
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|PDB= 1w27 |SIZE=350|CAPTION= <scene name='initialview01'>1w27</scene>, resolution 1.70Å | |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> | |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> | + | |LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w27 OCA], [http://www.ebi.ac.uk/pdbsum/1w27 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w27 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ritter, H.]] | [[Category: Ritter, H.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: DTT]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
[[Category: mio]] | [[Category: mio]] | ||
[[Category: phenylpropanoid metabolism]] | [[Category: phenylpropanoid metabolism]] | ||
| - | ''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 00:30:07 2008'' |
Revision as of 21:30, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Phenylalanine ammonia-lyase, with EC number 4.3.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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