1oas

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[[Image:1oas.gif|left|200px]]
[[Image:1oas.gif|left|200px]]
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{{Structure
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|PDB= 1oas |SIZE=350|CAPTION= <scene name='initialview01'>1oas</scene>, resolution 2.200&Aring;
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The line below this paragraph, containing "STRUCTURE_1oas", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1oas| PDB=1oas | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oas OCA], [http://www.ebi.ac.uk/pdbsum/1oas PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oas RCSB]</span>
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}}
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'''O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM'''
'''O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM'''
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[[Category: Rao, G S.J.]]
[[Category: Rao, G S.J.]]
[[Category: Schnackerz, K D.]]
[[Category: Schnackerz, K D.]]
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[[Category: beta replacement enzyme]]
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[[Category: Beta replacement enzyme]]
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[[Category: cystein biosynthesis]]
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[[Category: Cystein biosynthesis]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: plp dependent enzyme]]
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[[Category: Plp dependent enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:25 2008''
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Revision as of 00:36, 3 May 2008

Image:1oas.gif

Template:STRUCTURE 1oas

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 Page seeded by OCA on Sat May 3 03:36:23 2008

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