1oas
From Proteopedia
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|PDB= 1oas |SIZE=350|CAPTION= <scene name='initialview01'>1oas</scene>, resolution 2.200Å | |PDB= 1oas |SIZE=350|CAPTION= <scene name='initialview01'>1oas</scene>, resolution 2.200Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5 | + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] | |ACTIVITY= [http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] | ||
|GENE= | |GENE= | ||
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[[Category: plp dependent enzyme]] | [[Category: plp dependent enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:02:08 2008'' |
Revision as of 11:02, 23 March 2008
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| , resolution 2.200Å | |||||||
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| Ligands: | |||||||
| Activity: | Cysteine synthase, with EC number 2.5.1.47 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM
Overview
The last step in cysteine biosynthesis in enteric bacteria is catalyzed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase. Here we report the crystal structure at 2.2 A resolution of the A-isozyme of O-acetylserine sulfhydrylase isolated from Salmonella typhimurium. O-acetylserine sulfhydrylase shares the same fold with tryptophan synthase-beta from Salmonella typhimurium but the sequence identity level is below 20%. There are some major structural differences: the loops providing the interface to the alpha-subunit in tryptophan synthase-beta and two surface helices of tryptophan synthase-beta are missing in O-acetylserine sulfhydrylase. The hydrophobic channel for indole transport from the alpha to the beta active site of tryptophan synthase-beta is, not unexpectedly, also absent in O-acetylserine sulfhydrylase. The dimer interface, on the other hand, is more or less conserved in the two enzymes. The active site cleft of O-acetylserine sulfhydrylase is wider and therefore more exposed to the solvent. A possible binding site for the substrate O-acetylserine is discussed.
About this Structure
1OAS is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium., Burkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, Jansonius JN, J Mol Biol. 1998;283(1):121-33. PMID:9761678
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