2o7f
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2o7f |SIZE=350|CAPTION= <scene name='initialview01'>2o7f</scene>, resolution 2.0Å | |PDB= 2o7f |SIZE=350|CAPTION= <scene name='initialview01'>2o7f</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC ACID'>HC4</scene> | + | |LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC+ACID'>HC4</scene>, <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-5-HYDROXY-4-METHYL-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= hutH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | |GENE= hutH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2o6y|2o6y]], [[1gkm|1gkm]], [[1w27|1w27]], [[1y2m|1y2m]], [[1t6j|1t6j]], [[2nyn|2nyn]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7f OCA], [http://www.ebi.ac.uk/pdbsum/2o7f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o7f RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Moore, B S.]] | [[Category: Moore, B S.]] | ||
[[Category: Noel, J P.]] | [[Category: Noel, J P.]] | ||
| - | [[Category: HC4]] | ||
[[Category: methylidene imidazolone prosthetic group]] | [[Category: methylidene imidazolone prosthetic group]] | ||
| - | ''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 04:13:57 2008'' |
Revision as of 01:14, 31 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | hutH (Rhodobacter sphaeroides) | ||||||
| Related: | 2o6y, 1gkm, 1w27, 1y2m, 1t6j, 2nyn
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), complexed with coumaric acid
Overview
Aromatic amino acid ammonia-lyases catalyze the deamination of L-His, L-Phe, and L-Tyr, yielding ammonia plus aryl acids bearing an alpha,beta-unsaturated propenoic acid. We report crystallographic analyses of unliganded Rhodobacter sphaeroides tyrosine ammonia-lyase (RsTAL) and RsTAL bound to p-coumarate and caffeate. His 89 of RsTAL forms a hydrogen bond with the p-hydroxyl moieties of coumarate and caffeate. His 89 is conserved in TALs but replaced in phenylalanine ammonia-lyases (PALs) and histidine ammonia-lyases (HALs). Substitution of His 89 by Phe, a characteristic residue of PALs, yields a mutant with a switch in kinetic preference from L-Tyr to L-Phe. Structures of the H89F mutant in complex with the PAL product, cinnamate, or the PAL-specific inhibitor, 2-aminoindan-2-phosphonate (AIP), support the role of position 89 as a specificity determinant in the family of aromatic amino acid ammonia-lyases and aminomutases responsible for beta-amino acid biosynthesis.
About this Structure
2O7F is a Single protein structure of sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
Reference
Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases., Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP, Chem Biol. 2006 Dec;13(12):1327-38. PMID:17185228
Page seeded by OCA on Mon Mar 31 04:13:57 2008
