2yas

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{{STRUCTURE_2yas| PDB=2yas | SCENE= }}
{{STRUCTURE_2yas| PDB=2yas | SCENE= }}
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'''HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS COMPLEXED WITH RHODANIDE'''
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===HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS COMPLEXED WITH RHODANIDE===
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==Overview==
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The 3D structures of complexes between the hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) and several substrate and/or inhibitor molecules, including trichloracetaldehyde, hexafluoracetone, acetone, and rhodanide, were determined by X-ray crystallography. The complex with trichloracetaldehyde showed a covalent linkage between the protein and the inhibitor, which had apparently resulted from nucleophilic attack of the catalytic Ser80-Ogamma. All other complexes showed the substrate or inhibitor molecule merely hydrogen bonded to the protein. In addition, the native crystal structure of Hb-HNL was redetermined at cryo-temperature and at room temperature, eliminating previous uncertainties concerning residual electron density within the active site, and leading to the observation of two conserved water molecules. One of them was found to be conserved in all complex structures and appears to have mainly structural significance. The other water molecule is conserved in all structures except for the complex with rhodanide; it is hydrogen bonded to the imidazole of the catalytic His235 and appears to affect the Hb-HNL catalyzed reaction. The observed 3D structural data suggest implications for the enzyme mechanism. It appears that the enzyme-catalyzed cyanohydrin formation is unlikely to proceed via a hemiacetal or hemiketal intermediate covalently attached to the enzyme, despite the observation of such an intermediate for the complex with trichloracetaldehyde. Instead, the data are consistent with a mechanism where the incoming substrate is activated by hydrogen bonding with its carbonyl oxygen to the Ser80 and Thr11 hydroxy groups. A hydrogen cyanide molecule subsequently replaces a water molecule and is deprotonated presumably by the His235 base. Deprotonation is facilitated by the proximity of the positive charge of the Lys236 side chain.
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{{ABSTRACT_PUBMED_10548044}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis., Zuegg J, Gruber K, Gugganig M, Wagner UG, Kratky C, Protein Sci. 1999 Oct;8(10):1990-2000. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10548044 10548044]
Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis., Zuegg J, Gruber K, Gugganig M, Wagner UG, Kratky C, Protein Sci. 1999 Oct;8(10):1990-2000. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10548044 10548044]
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Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis., Wagner UG, Hasslacher M, Griengl H, Schwab H, Kratky C, Structure. 1996 Jul 15;4(7):811-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8805565 8805565]
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Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. Functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue., Hasslacher M, Schall M, Hayn M, Griengl H, Kohlwein SD, Schwab H, J Biol Chem. 1996 Mar 8;271(10):5884-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8621461 8621461]
[[Category: Hevea brasiliensis]]
[[Category: Hevea brasiliensis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Oxynitrilase]]
[[Category: Oxynitrilase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:11:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:26:06 2008''

Revision as of 18:26, 27 July 2008

Image:2yas.png

Template:STRUCTURE 2yas

HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS COMPLEXED WITH RHODANIDE

Template:ABSTRACT PUBMED 10548044

About this Structure

2YAS is a Single protein structure of sequence from Hevea brasiliensis. Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis., Zuegg J, Gruber K, Gugganig M, Wagner UG, Kratky C, Protein Sci. 1999 Oct;8(10):1990-2000. PMID:10548044

Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis., Wagner UG, Hasslacher M, Griengl H, Schwab H, Kratky C, Structure. 1996 Jul 15;4(7):811-22. PMID:8805565

Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. Functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue., Hasslacher M, Schall M, Hayn M, Griengl H, Kohlwein SD, Schwab H, J Biol Chem. 1996 Mar 8;271(10):5884-91. PMID:8621461

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