1tht: Difference between revisions
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'''STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI''' | {{Structure | ||
|PDB= 1tht |SIZE=350|CAPTION= <scene name='initialview01'>1tht</scene>, resolution 2.1Å | |||
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'''STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1THT is a [ | 1THT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THT OCA]. | ||
==Reference== | ==Reference== | ||
Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi., Lawson DM, Derewenda U, Serre L, Ferri S, Szittner R, Wei Y, Meighen EA, Derewenda ZS, Biochemistry. 1994 Aug 16;33(32):9382-8. PMID:[http:// | Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi., Lawson DM, Derewenda U, Serre L, Ferri S, Szittner R, Wei Y, Meighen EA, Derewenda ZS, Biochemistry. 1994 Aug 16;33(32):9382-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8068614 8068614] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio harveyi]] | [[Category: Vibrio harveyi]] | ||
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[[Category: thioesterase]] | [[Category: thioesterase]] | ||
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Revision as of 15:18, 20 March 2008
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STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI
OverviewOverview
The crystal structure of a myristoyl acyl carrier protein specific thioesterase (C14ACP-TE) from a bioluminescent bacterium, Vibrio harveyi, was solved by multiple isomorphous replacement methods and refined to an R factor of 22% at 2.1-A resolution. This is the first elucidation of a three-dimensional structure of a thioesterase. The overall tertiary architecture of the enzyme resembles closely the consensus fold of the rapidly expanding superfamily of alpha/beta hydrolases, although there is no detectable homology with any of its members at the amino acid sequence level. Particularly striking similarity exists between the C14ACP-TE structure and that of haloalkane dehalogenase from Xanthobacter autotrophicus. Contrary to the conclusions of earlier studies [Ferri, S. R., & Meighen, E. A. (1991) J. Biol. Chem. 266, 12852-12857] which implicated Ser77 in catalysis, the crystal structure of C14ACP-TE reveals a lipase-like catalytic triad made up of Ser114, His241, and Asp211. Surprisingly, the gamma-turn with Ser114 in a strained secondary conformation (phi = 53 degrees, psi = -127 degrees), characteristic of the so-called nucleophilic elbow, does not conform to the frequently invoked lipase/esterase consensus sequence (Gly-X-Ser-X-Gly), as the positions of both glycines are occupied by larger amino acids. Site-directed mutagenesis and radioactive labeling support the catalytic function of Ser114. Crystallographic analysis of the Ser77-->Gly mutant at 2.5-A resolution revealed no structural changes; in both cases the loop containing the residue in position 77 is disordered.(ABSTRACT TRUNCATED AT 250 WORDS)
About this StructureAbout this Structure
1THT is a Single protein structure of sequence from Vibrio harveyi. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi., Lawson DM, Derewenda U, Serre L, Ferri S, Szittner R, Wei Y, Meighen EA, Derewenda ZS, Biochemistry. 1994 Aug 16;33(32):9382-8. PMID:8068614
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