2uv8

From Proteopedia

Jump to: navigation, search
Warning: this is a large structure, and loading might take a long time or not happen at all.
2uv8, resolution 3.10Å ()
Ligands:
Non-Standard Residues:
Activity: Fatty-acyl-CoA synthase, with EC number 2.3.1.86
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

CRYSTAL STRUCTURE OF YEAST FATTY ACID SYNTHASE WITH STALLED ACYL CARRIER PROTEIN AT 3.1 ANGSTROM RESOLUTION

Publication Abstract from PubMed

In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.

Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase., Leibundgut M, Jenni S, Frick C, Ban N, Science. 2007 Apr 13;316(5822):288-90. PMID:17431182

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2uv8 is a 6 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

See Also

Reference

  • Leibundgut M, Jenni S, Frick C, Ban N. Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase. Science. 2007 Apr 13;316(5822):288-90. PMID:17431182 doi:316/5822/288

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools