1mla
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(New page: 200px<br /><applet load="1mla" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mla, resolution 1.5Å" /> '''THE ESCHERICHIA COLI ...)
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Revision as of 19:22, 20 November 2007
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THE ESCHERICHIA COLI MALONYL-COA:ACYL CARRIER PROTEIN TRANSACYLASE AT 1.5-ANGSTROMS RESOLUTION. CRYSTAL STRUCTURE OF A FATTY ACID SYNTHASE COMPONENT
Overview
Endogenous fatty acids are synthesized in all organisms in a pathway, catalyzed by the fatty acid synthase complex. In bacteria, where the fatty, acids are used primarily for incorporation into components of cell, membranes, fatty acid synthase is made up of several independent, cytoplasmic enzymes, each catalyzing one specific reaction. The initiation, of the elongation step, which extends the length of the growing acyl chain, by two carbons, requires the transfer of the malonyl moiety from, malonyl-CoA onto the acyl carrier protein. We report here the crystal, structure (refined at 1.5-A resolution to an R factor of 0.19) of the, malonyl-CoA specific transferase from Escherichia coli. The protein has an, alpha/beta type architecture, but its fold is unique. The active site, inferred from the location of the catalytic Ser-92 contains a typical, nucleophilic elbow as observed in alpha/beta hydrolases. Serine 92 is, hydrogen bonded to His-201 in a fashion similar to various serine, hydrolases. However, instead of a carboxyl acid typically found in, catalytic triads, the main chain carbonyl of Gln-250 serves as a hydrogen, bond acceptor in an interaction with His-201. Two other residues, Arg-117, and Glu-11, are also located in the active site, although their function, is not clear.
About this Structure
1MLA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component., Serre L, Verbree EC, Dauter Z, Stuitje AR, Derewenda ZS, J Biol Chem. 1995 Jun 2;270(22):12961-4. PMID:7768883
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