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| {{STRUCTURE_1oas| PDB=1oas | SCENE= }} | | {{STRUCTURE_1oas| PDB=1oas | SCENE= }} |
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| '''O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM'''
| | ===O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_9761678}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9761678 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9761678}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Homodimer]] | | [[Category: Homodimer]] |
| [[Category: Plp dependent enzyme]] | | [[Category: Plp dependent enzyme]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:48:06 2008'' |
