2uv9: Difference between revisions

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==Overview==

We report crystal structures of the 2.6-megadalton alpha6beta6, heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1, angstrom resolution. The alpha and beta polypeptide chains form the six, catalytic domains required for fatty acid synthesis and numerous expansion, segments responsible for extensive intersubunit connections. Detailed, views of all active sites provide insights into substrate specificities, and catalytic mechanisms and reveal their unique characteristics, which, are due to the integration into the multienzyme. The mode of acyl carrier, protein attachment in the reaction chamber, together with the spatial, distribution of active sites, suggests that iterative substrate shuttling, is achieved by a relatively restricted circular motion of the carrier, domain in the multifunctional enzyme.

We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.

==About this Structure==

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[[Category: transferase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:36 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-We report crystal structures of the 2.6-megadalton alpha6beta6, heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1, angstrom resolution. The alpha and beta polypeptide chains form the six, catalytic domains required for fatty acid synthesis and numerous expansion, segments responsible for extensive intersubunit connections. Detailed, views of all active sites provide insights into substrate specificities, and catalytic mechanisms and reveal their unique characteristics, which, are due to the integration into the multienzyme. The mode of acyl carrier, protein attachment in the reaction chamber, together with the spatial, distribution of active sites, suggests that iterative substrate shuttling, is achieved by a relatively restricted circular motion of the carrier, domain in the multifunctional enzyme.
+We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.
 ==About this Structure==
@@ Line 33: / Line 33: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:20:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:36 2008''