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1wkv
From Proteopedia
(New page: 200px<br /><applet load="1wkv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wkv, resolution 2.0Å" /> '''Crystal structure of ...) |
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| - | [[Image:1wkv.gif|left|200px]]<br /><applet load="1wkv" size=" | + | [[Image:1wkv.gif|left|200px]]<br /><applet load="1wkv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wkv, resolution 2.0Å" /> | caption="1wkv, resolution 2.0Å" /> | ||
'''Crystal structure of O-phosphoserine sulfhydrylase'''<br /> | '''Crystal structure of O-phosphoserine sulfhydrylase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic | + | O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine synthetic reaction from O-phospho-l-serine and sulfide. The crystal structure of the enzyme was determined at 2.0A resolution using the method of multi-wavelength anomalous dispersion. A monomer consists of three domains, including an N-terminal domain with a new alpha/beta fold. The topology folds of the middle and C-terminal domains were similar to those of the O-acetylserine sulfhydrylase-A from Salmonella typhimurium and the cystathionine beta-synthase from human. The cofactor, pyridoxal 5'-phosphate, is bound in a cleft between the middle and C-terminal domains through a covalent linkage to Lys127. Based on the structure determined, O-phospho-l-serine could be rationally modeled into the active site of the enzyme. An enzyme-substrate complex model and a mutation experiment revealed that Arg297, unique to hyperthermophilic archaea, is one of the most crucial residues for O-phosphoserine sulfhydrylation activity. There are more hydrophobic areas and less electric charges at the dimer interface, compared to the S.typhimurium O-acetylserine sulfhydrylase. |
==About this Structure== | ==About this Structure== | ||
| - | 1WKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with ACT and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1WKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: open alpha/beta folding]] | [[Category: open alpha/beta folding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:27 2008'' |
Revision as of 13:45, 21 February 2008
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Crystal structure of O-phosphoserine sulfhydrylase
Overview
O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine synthetic reaction from O-phospho-l-serine and sulfide. The crystal structure of the enzyme was determined at 2.0A resolution using the method of multi-wavelength anomalous dispersion. A monomer consists of three domains, including an N-terminal domain with a new alpha/beta fold. The topology folds of the middle and C-terminal domains were similar to those of the O-acetylserine sulfhydrylase-A from Salmonella typhimurium and the cystathionine beta-synthase from human. The cofactor, pyridoxal 5'-phosphate, is bound in a cleft between the middle and C-terminal domains through a covalent linkage to Lys127. Based on the structure determined, O-phospho-l-serine could be rationally modeled into the active site of the enzyme. An enzyme-substrate complex model and a mutation experiment revealed that Arg297, unique to hyperthermophilic archaea, is one of the most crucial residues for O-phosphoserine sulfhydrylation activity. There are more hydrophobic areas and less electric charges at the dimer interface, compared to the S.typhimurium O-acetylserine sulfhydrylase.
About this Structure
1WKV is a Single protein structure of sequence from Aeropyrum pernix with and as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution., Oda Y, Mino K, Ishikawa K, Ataka M, J Mol Biol. 2005 Aug 12;351(2):334-44. PMID:16005886
Page seeded by OCA on Thu Feb 21 15:45:27 2008
Categories: Aeropyrum pernix | Single protein | Ataka, M. | Ishikawa, K. | Mino, K. | Oda, Y. | ACT | PLP | Homodimer | Open alpha/beta folding
