Sandbox Reserved 914: Difference between revisions
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== Structure == | == Structure == | ||
The secondary structure of PPT1 contains several α-helices and few β-sheets (Figure 1). PPT1 includes residues 28-306, after the 27-residue signal peptide has been removed <ref name="RSCB"> | The secondary structure of PPT1 contains several α-helices and few β-sheets (Figure 1). PPT1 includes residues 28-306, after the 27-residue signal peptide has been removed <ref name="RSCB">PMID:10781062</ref>. An insertion is found between β6 and β7, residues 140-223, and that forms a <scene name='57/573128/9/1'>second domain</scene>, shown in blue, that is compromised almost entirely of the fatty acid binding site. This second domain region contains six helices, α2-α7<ref name="RSCB"/>. | ||
The α/β hydrolase fold is common to many other hydrolases <ref name="RSCB"/>. The α/β hydrolase fold has a central 6 stranded parallel β-sheet consisting of <scene name='57/573128/4/1'>β3-β8</scene> and α-helices <scene name='57/573128/5/1'>αA, αB, αC, and αF</scene><ref name="RSCB"/>. A catalytic triad and an oxyanion hole are also common features to the PPT1 protein family. None of the enzymes within the α/β hydrolase fold family require a cofactor for catalytic activity. | The α/β hydrolase fold is common to many other hydrolases <ref name="RSCB"/>. The α/β hydrolase fold has a central 6 stranded parallel β-sheet consisting of <scene name='57/573128/4/1'>β3-β8</scene> and α-helices <scene name='57/573128/5/1'>αA, αB, αC, and αF</scene><ref name="RSCB"/>. A catalytic triad and an oxyanion hole are also common features to the PPT1 protein family. None of the enzymes within the α/β hydrolase fold family require a cofactor for catalytic activity. | ||
